ASF1_YEAST
ID ASF1_YEAST Reviewed; 279 AA.
AC P32447; D6VW69;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Histone chaperone ASF1;
DE AltName: Full=Anti-silencing function protein 1;
DE Short=yASF1;
GN Name=ASF1 {ECO:0000303|PubMed:9290207};
GN Synonyms=CIA1 {ECO:0000303|PubMed:11856374};
GN OrderedLocusNames=YJL115W {ECO:0000312|SGD:S000003651}; ORFNames=J0755;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9290207;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1029::aid-yea160>3.0.co;2-1;
RA Le S., Davis C., Konopka J.B., Sternglanz R.;
RT "Two new S-phase-specific genes from Saccharomyces cerevisiae.";
RL Yeast 13:1029-1042(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION.
RX PubMed=10591219; DOI=10.1038/990147;
RA Tyler J.K., Adams C.R., Chen S.-R., Kobayashi R., Kamakaka R.T.,
RA Kadonaga J.T.;
RT "The RCAF complex mediates chromatin assembly during DNA replication and
RT repair.";
RL Nature 402:555-560(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH HISTONE H3; HISTONE H4; HIR1 AND HIR2.
RX PubMed=11412995; DOI=10.1016/s0960-9822(01)00140-3;
RA Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D.;
RT "Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for
RT heterochromatic silencing.";
RL Curr. Biol. 11:463-473(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH RAD53.
RX PubMed=11331602; DOI=10.1101/gad.873201;
RA Hu F., Alcasabas A.A., Elledge S.J.;
RT "Asf1 links Rad53 to control of chromatin assembly.";
RL Genes Dev. 15:1061-1066(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH SAS2; SAS4 AND SAS5.
RX PubMed=11731479; DOI=10.1101/gad.907201;
RA Osada S., Sutton A., Muster N., Brown C.E., Yates J.R. III, Sternglanz R.,
RA Workman J.L.;
RT "The yeast SAS (something about silencing) protein complex contains a MYST-
RT type putative acetyltransferase and functions with chromatin assembly
RT factor ASF1.";
RL Genes Dev. 15:3155-3168(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH SAS2; SAS4 AND SAS5.
RX PubMed=11731480; DOI=10.1101/gad.929001;
RA Meijsing S.H., Ehrenhofer-Murray A.E.;
RT "The silencing complex SAS-I links histone acetylation to the assembly of
RT repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae.";
RL Genes Dev. 15:3169-3182(2001).
RN [11]
RP FUNCTION, INTERACTION WITH HIR1, AND SUBCELLULAR LOCATION.
RX PubMed=11404324; DOI=10.1093/genetics/158.2.587;
RA Sutton A., Bucaria J., Osley M.A., Sternglanz R.;
RT "Yeast ASF1 protein is required for cell cycle regulation of histone gene
RT transcription.";
RL Genetics 158:587-596(2001).
RN [12]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HISTONE
RP H3; HISTONE H4 AND RAD53.
RX PubMed=11172707; DOI=10.1016/s1097-2765(01)00150-2;
RA Emili A., Schieltz D.M., Yates J.R. III, Hartwell L.H.;
RT "Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin
RT assembly factor Asf1.";
RL Mol. Cell 7:13-20(2001).
RN [13]
RP FUNCTION, AND INTERACTION WITH HISTONE H3 AND HISTONE H4.
RX PubMed=11856374; DOI=10.1046/j.1356-9597.2001.00493.x;
RA Umehara T., Chimura T., Ichikawa N., Horikoshi M.;
RT "Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional
RT both in vivo and in vitro.";
RL Genes Cells 7:59-73(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH CAC2; HISTONE H3 AND HISTONE H4.
RX PubMed=11756556; DOI=10.1128/mcb.22.2.614-625.2002;
RA Krawitz D.C., Kama T., Kaufman P.D.;
RT "Chromatin assembly factor I mutants defective for PCNA binding require
RT Asf1/Hir proteins for silencing.";
RL Mol. Cell. Biol. 22:614-625(2002).
RN [15]
RP FUNCTION, AND INTERACTION WITH BDF1; BDF2; SPT15; TAF1 AND TAF7.
RX PubMed=12093919; DOI=10.1073/pnas.142627899;
RA Chimura T., Kuzuhara T., Horikoshi M.;
RT "Identification and characterization of CIA/ASF1 as an interactor of
RT bromodomains associated with TFIID.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002).
RN [16]
RP INTERACTION WITH RAD53.
RX PubMed=12851493;
RA Schwartz M.F., Lee S.-J., Duong J.K., Eminaga S., Stern D.F.;
RT "FHA domain-mediated DNA checkpoint regulation of Rad53.";
RL Cell Cycle 2:384-396(2003).
RN [17]
RP INTERACTION WITH HISTONE H3 AND HISTONE H4.
RX PubMed=12626510; DOI=10.1074/jbc.m210709200;
RA Sutton A., Shia W.-J., Band D., Kaufman P.D., Osada S., Workman J.L.,
RA Sternglanz R.;
RT "Sas4 and Sas5 are required for the histone acetyltransferase activity of
RT Sas2 in the SAS complex.";
RL J. Biol. Chem. 278:16887-16892(2003).
RN [18]
RP INTERACTION WITH RAD53.
RX PubMed=12917350; DOI=10.1128/mcb.23.17.6300-6314.2003;
RA Lee S.-J., Schwartz M.F., Duong J.K., Stern D.F.;
RT "Rad53 phosphorylation site clusters are important for Rad53 regulation and
RT signaling.";
RL Mol. Cell. Biol. 23:6300-6314(2003).
RN [19]
RP FUNCTION.
RX PubMed=14585955; DOI=10.1128/mcb.23.22.7937-7946.2003;
RA Robinson K.M., Schultz M.C.;
RT "Replication-independent assembly of nucleosome arrays in a novel yeast
RT chromatin reconstitution system involves antisilencing factor Asf1p and
RT chromodomain protein Chd1p.";
RL Mol. Cell. Biol. 23:7937-7946(2003).
RN [20]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [21]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [22]
RP FUNCTION.
RX PubMed=15071494; DOI=10.1038/sj.embor.7400128;
RA Prado F., Cortes-Ledesma F., Aguilera A.;
RT "The absence of the yeast chromatin assembly factor Asf1 increases genomic
RT instability and sister chromatid exchange.";
RL EMBO Rep. 5:497-502(2004).
RN [23]
RP FUNCTION.
RX PubMed=15452122; DOI=10.1074/jbc.m406113200;
RA Adkins M.W., Tyler J.K.;
RT "The histone chaperone Asf1p mediates global chromatin disassembly in
RT vivo.";
RL J. Biol. Chem. 279:52069-52074(2004).
RN [24]
RP FUNCTION.
RX PubMed=15175160; DOI=10.1016/j.molcel.2004.05.016;
RA Adkins M.W., Howar S.R., Tyler J.K.;
RT "Chromatin disassembly mediated by the histone chaperone Asf1 is essential
RT for transcriptional activation of the yeast PHO5 and PHO8 genes.";
RL Mol. Cell 14:657-666(2004).
RN [25]
RP FUNCTION.
RX PubMed=15542829; DOI=10.1128/mcb.24.23.10180-10192.2004;
RA Glowczewski L., Waterborg J.H., Berman J.G.;
RT "Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms
RT of histone H4 from chromatin and the nucleus.";
RL Mol. Cell. Biol. 24:10180-10192(2004).
RN [26]
RP FUNCTION.
RX PubMed=15542840; DOI=10.1128/mcb.24.23.10313-10327.2004;
RA Ramey C.J., Howar S., Adkins M., Linger J., Spicer J., Tyler J.K.;
RT "Activation of the DNA damage checkpoint in yeast lacking the histone
RT chaperone anti-silencing function 1.";
RL Mol. Cell. Biol. 24:10313-10327(2004).
RN [27]
RP FUNCTION.
RX PubMed=15766286; DOI=10.1021/bi047523u;
RA Robinson K.M., Schultz M.C.;
RT "Gal4-VP16 directs ATP-independent chromatin reorganization in a yeast
RT chromatin assembly system.";
RL Biochemistry 44:4551-4561(2005).
RN [28]
RP FUNCTION, INTERACTION WITH HIR1; HIR2; HIR3; HPC2; HISTONE H3; HISTONE H4
RP AND RAD53, AND MUTAGENESIS OF 36-HIS-ASP-37.
RX PubMed=16303565; DOI=10.1016/j.cub.2005.10.053;
RA Green E.M., Antczak A.J., Bailey A.O., Franco A.A., Wu K.J.,
RA Yates J.R. III, Kaufman P.D.;
RT "Replication-independent histone deposition by the HIR complex and Asf1.";
RL Curr. Biol. 15:2044-2049(2005).
RN [29]
RP FUNCTION.
RX PubMed=15821127; DOI=10.1128/ec.4.4.673-684.2005;
RA Harkness T.A.A., Arnason T.G., Legrand C., Pisclevich M.G., Davies G.F.,
RA Turner E.L.;
RT "Contribution of CAF-I to anaphase-promoting-complex-mediated mitotic
RT chromatin assembly in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:673-684(2005).
RN [30]
RP FUNCTION, AND INTERACTION WITH RFC1; RFC2; RFC3; RFC4 AND RFC5.
RX PubMed=15901673; DOI=10.1101/gad.1305005;
RA Franco A.A., Lam W.M., Burgers P.M., Kaufman P.D.;
RT "Histone deposition protein Asf1 maintains DNA replisome integrity and
RT interacts with replication factor C.";
RL Genes Dev. 19:1365-1375(2005).
RN [31]
RP FUNCTION, INTERACTION WITH RAD53, AND SUBCELLULAR LOCATION.
RX PubMed=16020781; DOI=10.1534/genetics.105.044719;
RA Sharp J.A., Rizki G., Kaufman P.D.;
RT "Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage
RT checkpoint kinases in Saccharomyces cerevisiae.";
RL Genetics 171:885-899(2005).
RN [32]
RP FUNCTION.
RX PubMed=16143623; DOI=10.1534/genetics.105.043000;
RA Linger J., Tyler J.K.;
RT "The yeast histone chaperone chromatin assembly factor 1 protects against
RT double-strand DNA-damaging agents.";
RL Genetics 171:1513-1522(2005).
RN [33]
RP FUNCTION.
RX PubMed=16039596; DOI=10.1016/j.molcel.2005.05.028;
RA Schermer U.J., Korber P., Hoerz W.;
RT "Histones are incorporated in trans during reassembly of the yeast PHO5
RT promoter.";
RL Mol. Cell 19:279-285(2005).
RN [34]
RP FUNCTION.
RX PubMed=15632066; DOI=10.1128/mcb.25.2.652-660.2005;
RA Zabaronick S.R., Tyler J.K.;
RT "The histone chaperone anti-silencing function 1 is a global regulator of
RT transcription independent of passage through S phase.";
RL Mol. Cell. Biol. 25:652-660(2005).
RN [35]
RP ERRATUM OF PUBMED:15632066.
RA Zabaronick S.R., Tyler J.K.;
RL Mol. Cell. Biol. 25:2871-2871(2005).
RN [36]
RP FUNCTION.
RX PubMed=15891116; DOI=10.1093/nar/gki560;
RA Osada S., Kurita M., Nishikawa J., Nishihara T.;
RT "Chromatin assembly factor Asf1p-dependent occupancy of the SAS histone
RT acetyltransferase complex at the silent mating-type locus HMLalpha.";
RL Nucleic Acids Res. 33:2742-2750(2005).
RN [37]
RP FUNCTION.
RX PubMed=16141196; DOI=10.1093/nar/gki806;
RA Lewis L.K., Karthikeyan G., Cassiano J., Resnick M.A.;
RT "Reduction of nucleosome assembly during new DNA synthesis impairs both
RT major pathways of double-strand break repair.";
RL Nucleic Acids Res. 33:4928-4939(2005).
RN [38]
RP FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, AND MUTAGENESIS OF
RP ASP-37; GLU-39; ASP-54; VAL-94 AND ARG-108.
RX PubMed=15840725; DOI=10.1073/pnas.0500149102;
RA Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R.,
RA Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C., Ochsenbein F.;
RT "Structural basis for the interaction of Asf1 with histone H3 and its
RT functional implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005).
RN [39]
RP FUNCTION.
RX PubMed=16815704; DOI=10.1016/j.cub.2006.06.023;
RA Celic I., Masumoto H., Griffith W.P., Meluh P., Cotter R.J., Boeke J.D.,
RA Verreault A.;
RT "The sirtuins Hst3 and Hst4p preserve genome integrity by controlling
RT histone H3 lysine 56 deacetylation.";
RL Curr. Biol. 16:1280-1289(2006).
RN [40]
RP FUNCTION.
RX PubMed=16936140; DOI=10.1128/ec.00202-06;
RA Linger J., Tyler J.K.;
RT "Global replication-independent histone H4 exchange in budding yeast.";
RL Eukaryot. Cell 5:1780-1787(2006).
RN [41]
RP FUNCTION, INTERACTION WITH HISTONE H3 AND RAD53, AND MUTAGENESIS OF
RP VAL-152.
RX PubMed=16582440; DOI=10.1534/genetics.105.054783;
RA Tamburini B.A., Carson J.J., Linger J.G., Tyler J.K.;
RT "Dominant mutants of the Saccharomyces cerevisiae ASF1 histone chaperone
RT bypass the need for CAF-1 in transcriptional silencing by altering histone
RT and Sir protein recruitment.";
RL Genetics 173:599-610(2006).
RN [42]
RP FUNCTION.
RX PubMed=16407267; DOI=10.1074/jbc.m513340200;
RA Korber P., Barbaric S., Luckenbach T., Schmid A., Schermer U.J.,
RA Blaschke D., Hoerz W.;
RT "The histone chaperone Asf1 increases the rate of histone eviction at the
RT yeast PHO5 and PHO8 promoters.";
RL J. Biol. Chem. 281:5539-5545(2006).
RN [43]
RP FUNCTION.
RX PubMed=17046836; DOI=10.1074/jbc.c600265200;
RA Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A.;
RT "Rtt109 is required for proper H3K56 acetylation: a chromatin mark
RT associated with the elongating RNA polymerase II.";
RL J. Biol. Chem. 281:37270-37274(2006).
RN [44]
RP FUNCTION.
RX PubMed=16678113; DOI=10.1016/j.molcel.2006.03.014;
RA Schwabish M.A., Struhl K.;
RT "Asf1 mediates histone eviction and deposition during elongation by RNA
RT polymerase II.";
RL Mol. Cell 22:415-422(2006).
RN [45]
RP FUNCTION.
RX PubMed=16501045; DOI=10.1073/pnas.0511102103;
RA Kats E.S., Albuquerque C.P., Zhou H., Kolodner R.D.;
RT "Checkpoint functions are required for normal S-phase progression in
RT Saccharomyces cerevisiae RCAF- and CAF-I-defective mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3710-3715(2006).
RN [46]
RP FUNCTION, AND MUTAGENESIS OF VAL-45; 53-HIS-ASP-54; VAL-94; LEU-96;
RP TYR-112; ARG-145 AND THR-147.
RX PubMed=16627621; DOI=10.1073/pnas.0601676103;
RA Recht J., Tsubota T., Tanny J.C., Diaz R.L., Berger J.M., Zhang X.,
RA Garcia B.A., Shabanowitz J., Burlingame A.L., Hunt D.F., Kaufman P.D.,
RA Allis C.D.;
RT "Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a
RT modification associated with S phase in mitosis and meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6988-6993(2006).
RN [47]
RP FUNCTION, AND MUTAGENESIS OF SER-48; VAL-94; TYR-112; ARG-145 AND THR-147.
RX PubMed=17107956; DOI=10.1074/jbc.m608025200;
RA Adkins M.W., Carson J.J., English C.M., Ramey C.J., Tyler J.K.;
RT "The histone chaperone anti-silencing function 1 stimulates the acetylation
RT of newly synthesized histone H3 in S-phase.";
RL J. Biol. Chem. 282:1334-1340(2007).
RN [48]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [49]
RP FUNCTION, AND INTERACTION WITH RTT109.
RX PubMed=17320445; DOI=10.1016/j.molcel.2007.02.006;
RA Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A.,
RA Denu J.M., Kaufman P.D.;
RT "Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent
RT complexes.";
RL Mol. Cell 25:703-712(2007).
RN [50]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [51]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [52]
RP FUNCTION.
RX PubMed=21256037; DOI=10.1016/j.str.2010.12.012;
RA Tang Y., Holbert M.A., Delgoshaie N., Wurtele H., Guillemette B., Meeth K.,
RA Yuan H., Drogaris P., Lee E.H., Durette C., Thibault P., Verreault A.,
RA Cole P.A., Marmorstein R.;
RT "Structure of the Rtt109-AcCoA/Vps75 complex and implications for
RT chaperone-mediated histone acetylation.";
RL Structure 19:221-231(2011).
RN [53]
RP INTERACTION WITH HISTONE H3/H4 HETERODIMERS.
RX PubMed=27036862; DOI=10.1093/nar/gkw209;
RA Hammond C.M., Sundaramoorthy R., Larance M., Lamond A., Stevens M.A.,
RA El-Mkami H., Norman D.G., Owen-Hughes T.;
RT "The histone chaperone Vps75 forms multiple oligomeric assemblies capable
RT of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4
RT complexes.";
RL Nucleic Acids Res. 44:6157-6172(2016).
RN [54]
RP FUNCTION, INTERACTION WITH HISTONE H3/H4 HETERODIMERS, AND MUTAGENESIS OF
RP GLU-105.
RX PubMed=31194870; DOI=10.1093/nar/gkz508;
RA Cote J.M., Kuo Y.M., Henry R.A., Scherman H., Krzizike D.D., Andrews A.J.;
RT "Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56
RT acetylation.";
RL Nucleic Acids Res. 47:7380-7391(2019).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-154, FUNCTION, INTERACTION WITH
RP HISTONE H3; HISTONE H4 AND RAD53, AND MUTAGENESIS OF 36-HIS-ASP-37.
RX PubMed=14680630; DOI=10.1016/j.cub.2003.11.027;
RA Daganzo S.M., Erzberger J.P., Lam W.M., Skordalakes E., Zhang R.,
RA Franco A.A., Brill S.J., Adams P.D., Berger J.M., Kaufman P.D.;
RT "Structure and function of the conserved core of histone deposition protein
RT Asf1.";
RL Curr. Biol. 13:2148-2158(2003).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-169.
RX PubMed=16428312; DOI=10.1093/jb/mvi182;
RA Padmanabhan B., Kataoka K., Umehara T., Adachi N., Yokoyama S.,
RA Horikoshi M.;
RT "Structural similarity between histone chaperone Cia1p/Asf1p and DNA-
RT binding protein NF-kappaB.";
RL J. Biochem. 138:821-829(2005).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-169 IN COMPLEX WITH THE HISTONE
RP H3/H4 HETERODIMER, AND MUTAGENESIS OF LEU-6; SER-48; VAL-94; VAL-109;
RP TYR-112; ARG-145; VAL-146 AND THR-147.
RX PubMed=17081973; DOI=10.1016/j.cell.2006.08.047;
RA English C.M., Adkins M.W., Carson J.J., Churchill M.E.A., Tyler J.K.;
RT "Structural basis for the histone chaperone activity of Asf1.";
RL Cell 127:495-508(2006).
RN [58] {ECO:0007744|PDB:6F0Y}
RP STRUCTURE BY NMR OF 2-169, AND INTERACTION WITH RTT109 AND HISTONE H3/H4
RP HETERODIMERS.
RX PubMed=29300933; DOI=10.1093/nar/gkx1283;
RA Lercher L., Danilenko N., Kirkpatrick J., Carlomagno T.;
RT "Structural characterization of the Asf1-Rtt109 interaction and its role in
RT histone acetylation.";
RL Nucleic Acids Res. 46:2279-2289(2018).
RN [59] {ECO:0007744|PDB:6O22}
RP STRUCTURE BY NMR IN COMPLEX WITH RTT109 AND VPS75, AND INTERACTION WITH
RP RTT109; VPS75 AND H3/H4 HETERODIMERS.
RX PubMed=31387991; DOI=10.1038/s41467-019-11410-7;
RA Danilenko N., Lercher L., Kirkpatrick J., Gabel F., Codutti L.,
RA Carlomagno T.;
RT "Histone chaperone exploits intrinsic disorder to switch acetylation
RT specificity.";
RL Nat. Commun. 10:3435-3435(2019).
CC -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC histone exchange and removal during nucleosome assembly and disassembly
CC (PubMed:16936140, PubMed:16678113, PubMed:16407267, PubMed:16039596,
CC PubMed:15891116, PubMed:16303565, PubMed:15766286, PubMed:15542829,
CC PubMed:15175160, PubMed:15452122, PubMed:15071494, PubMed:11856374,
CC PubMed:11404324, PubMed:11331602, PubMed:11172707, PubMed:14680630).
CC Facilitates histone deposition through both replication-dependent and
CC replication-independent chromatin assembly pathways (PubMed:14585955,
CC PubMed:16678113, PubMed:15632066). Cooperates with chromatin assembly
CC factor 1 (CAF-1) to promote replication-dependent chromatin assembly
CC and with the HIR complex to promote replication-independent chromatin
CC assembly, which may occur during transcription and DNA repair
CC (PubMed:16501045, PubMed:16582440, PubMed:16141196, PubMed:16143623,
CC PubMed:16020781, PubMed:15821127, PubMed:16303565, PubMed:15542840,
CC PubMed:12093919, PubMed:11756556, PubMed:11404324, PubMed:11731480,
CC PubMed:11731479, PubMed:11412995, PubMed:10591219). May be required for
CC the maintenance of a subset of replication elongation factors,
CC including DNA polymerase epsilon, the RFC complex and PCNA, at stalled
CC replication forks (PubMed:15901673, PubMed:11412995). Also required for
CC RTT109-dependent acetylation of histone H3 on 'Lys-9' and 'Lys-56'
CC (PubMed:17320445, PubMed:17107956, PubMed:17046836, PubMed:16815704,
CC PubMed:16627621, PubMed:15840725, PubMed:21256037). Promotion of
CC RTT109-mediated histone H3 'Lys-56' acetylation is dependent on
CC interactions with histone H3 pre-acetylated on 'Lys-14'
CC (PubMed:31194870). {ECO:0000269|PubMed:10591219,
CC ECO:0000269|PubMed:11172707, ECO:0000269|PubMed:11331602,
CC ECO:0000269|PubMed:11404324, ECO:0000269|PubMed:11412995,
CC ECO:0000269|PubMed:11731479, ECO:0000269|PubMed:11731480,
CC ECO:0000269|PubMed:11756556, ECO:0000269|PubMed:11856374,
CC ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:14585955,
CC ECO:0000269|PubMed:14680630, ECO:0000269|PubMed:15071494,
CC ECO:0000269|PubMed:15175160, ECO:0000269|PubMed:15452122,
CC ECO:0000269|PubMed:15542829, ECO:0000269|PubMed:15542840,
CC ECO:0000269|PubMed:15632066, ECO:0000269|PubMed:15766286,
CC ECO:0000269|PubMed:15821127, ECO:0000269|PubMed:15840725,
CC ECO:0000269|PubMed:15891116, ECO:0000269|PubMed:15901673,
CC ECO:0000269|PubMed:16020781, ECO:0000269|PubMed:16039596,
CC ECO:0000269|PubMed:16141196, ECO:0000269|PubMed:16143623,
CC ECO:0000269|PubMed:16303565, ECO:0000269|PubMed:16407267,
CC ECO:0000269|PubMed:16501045, ECO:0000269|PubMed:16582440,
CC ECO:0000269|PubMed:16627621, ECO:0000269|PubMed:16678113,
CC ECO:0000269|PubMed:16815704, ECO:0000269|PubMed:16936140,
CC ECO:0000269|PubMed:17046836, ECO:0000269|PubMed:17107956,
CC ECO:0000269|PubMed:17320445, ECO:0000269|PubMed:21256037,
CC ECO:0000269|PubMed:31194870}.
CC -!- SUBUNIT: Interacts with histone H3/H4 heterodimers via both histone H3
CC and histone H4 (PubMed:11172707, PubMed:11412995, PubMed:11856374,
CC PubMed:11756556, PubMed:12626510, PubMed:16303565, PubMed:15840725,
CC PubMed:16582440, PubMed:14680630, PubMed:17081973, PubMed:31387991,
CC PubMed:29300933, PubMed:27036862). Binds with higher affinity to H3/H4
CC heterodimers where histone H3 has been pre-acetylated on 'Lys-14'
CC (PubMed:31194870). Interacts with RAD53 and this may impair interaction
CC with histones and chromatin assembly; the interaction is reduced upon
CC activation of DNA damage or replication checkpoints which in turn
CC promotes histone binding and chromatin assembly (PubMed:11331602,
CC PubMed:12851493, PubMed:12917350, PubMed:16303565, PubMed:16020781,
CC PubMed:14680630). Interacts with the CAC2 subunit of chromatin assembly
CC factor 1 (CAF-1) (PubMed:11756556). Interacts with the HIR1, HIR2, HIR3
CC and HPC2 subunits of the HIR complex (PubMed:11404324, PubMed:11412995,
CC PubMed:16303565). Interacts with the RFC1, RFC2, RFC3, RFC4 and RFC5
CC subunits of the replication factor C (RF-C/RFC) complex; which may
CC recruit this protein to DNA (PubMed:15901673). Interacts with the SAS2,
CC SAS4 and SAS5 subunits of the SAS/SAS-I complex (PubMed:11731479,
CC PubMed:11731480). Interacts with the BDF1, BDF2, SPT15, TAF1 and TAF7
CC subunits of the TFIID complex (PubMed:12093919). Interacts with RTT109
CC and VPS75; the interaction with RTT109 is direct (PubMed:29300933,
CC PubMed:31387991, PubMed:17320445). {ECO:0000269|PubMed:11172707,
CC ECO:0000269|PubMed:11331602, ECO:0000269|PubMed:11404324,
CC ECO:0000269|PubMed:11412995, ECO:0000269|PubMed:11731479,
CC ECO:0000269|PubMed:11731480, ECO:0000269|PubMed:11756556,
CC ECO:0000269|PubMed:11856374, ECO:0000269|PubMed:12093919,
CC ECO:0000269|PubMed:12626510, ECO:0000269|PubMed:12851493,
CC ECO:0000269|PubMed:12917350, ECO:0000269|PubMed:14680630,
CC ECO:0000269|PubMed:15840725, ECO:0000269|PubMed:15901673,
CC ECO:0000269|PubMed:16020781, ECO:0000269|PubMed:16303565,
CC ECO:0000269|PubMed:16582440, ECO:0000269|PubMed:17081973,
CC ECO:0000269|PubMed:17320445, ECO:0000269|PubMed:27036862,
CC ECO:0000269|PubMed:29300933, ECO:0000269|PubMed:31194870,
CC ECO:0000269|PubMed:31387991}.
CC -!- INTERACTION:
CC P32447; P02309: HHF2; NbExp=5; IntAct=EBI-3003, EBI-8113;
CC P32447; P61830: HHT2; NbExp=4; IntAct=EBI-3003, EBI-8098;
CC P32447; P32479: HIR1; NbExp=6; IntAct=EBI-3003, EBI-8316;
CC P32447; P22216: RAD53; NbExp=10; IntAct=EBI-3003, EBI-17843;
CC P32447; P40161: RTT106; NbExp=5; IntAct=EBI-3003, EBI-29119;
CC P32447; P40963: SAS2; NbExp=4; IntAct=EBI-3003, EBI-16476;
CC P32447; Q04003: SAS4; NbExp=5; IntAct=EBI-3003, EBI-38500;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11404324,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16020781}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks in S-phase (at the RNA level).
CC {ECO:0000269|PubMed:9290207}.
CC -!- MISCELLANEOUS: Present with 6230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; L07593; AAC37512.1; -; Genomic_DNA.
DR EMBL; Z49390; CAA89410.1; -; Genomic_DNA.
DR EMBL; AY557874; AAS56200.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08685.1; -; Genomic_DNA.
DR PIR; S30766; S30766.
DR RefSeq; NP_012420.1; NM_001181548.1.
DR PDB; 1ROC; X-ray; 1.50 A; A=2-154.
DR PDB; 1WG3; X-ray; 3.00 A; A=1-169.
DR PDB; 2HUE; X-ray; 1.70 A; A=2-169.
DR PDB; 2IDC; X-ray; 2.20 A; A=2-155.
DR PDB; 2YGV; X-ray; 2.94 A; A/B/C/D=1-156.
DR PDB; 4EO5; X-ray; 2.35 A; A=2-169.
DR PDB; 4ZBJ; X-ray; 2.25 A; A=2-169.
DR PDB; 5EII; X-ray; 2.44 A; G/I=1-156.
DR PDB; 5UCB; X-ray; 1.52 A; B=2-154.
DR PDB; 5UEA; X-ray; 1.70 A; D/X=2-154.
DR PDB; 5UEK; X-ray; 1.70 A; A=2-154.
DR PDB; 6AYZ; X-ray; 2.10 A; A/M=2-154.
DR PDB; 6AZ2; X-ray; 2.48 A; B/D=2-154.
DR PDB; 6F0Y; NMR; -; A=2-169.
DR PDB; 6O22; Other; -; D=2-279.
DR PDBsum; 1ROC; -.
DR PDBsum; 1WG3; -.
DR PDBsum; 2HUE; -.
DR PDBsum; 2IDC; -.
DR PDBsum; 2YGV; -.
DR PDBsum; 4EO5; -.
DR PDBsum; 4ZBJ; -.
DR PDBsum; 5EII; -.
DR PDBsum; 5UCB; -.
DR PDBsum; 5UEA; -.
DR PDBsum; 5UEK; -.
DR PDBsum; 6AYZ; -.
DR PDBsum; 6AZ2; -.
DR PDBsum; 6F0Y; -.
DR PDBsum; 6O22; -.
DR AlphaFoldDB; P32447; -.
DR SASBDB; P32447; -.
DR SMR; P32447; -.
DR BioGRID; 33639; 646.
DR ComplexPortal; CPX-1322; RAD53-ASF1 complex.
DR DIP; DIP-2675N; -.
DR IntAct; P32447; 134.
DR MINT; P32447; -.
DR STRING; 4932.YJL115W; -.
DR iPTMnet; P32447; -.
DR MaxQB; P32447; -.
DR PaxDb; P32447; -.
DR PRIDE; P32447; -.
DR ABCD; P32447; 6 sequenced antibodies.
DR EnsemblFungi; YJL115W_mRNA; YJL115W; YJL115W.
DR GeneID; 853327; -.
DR KEGG; sce:YJL115W; -.
DR SGD; S000003651; ASF1.
DR VEuPathDB; FungiDB:YJL115W; -.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_0_2_1; -.
DR InParanoid; P32447; -.
DR OMA; SYDEREF; -.
DR BioCyc; YEAST:G3O-31569-MON; -.
DR Reactome; R-SCE-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR EvolutionaryTrace; P32447; -.
DR PRO; PR:P32447; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32447; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0070775; C:H3 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:SGD.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IMP:SGD.
DR GO; GO:0043486; P:histone exchange; IMP:SGD.
DR GO; GO:0033523; P:histone H2B ubiquitination; IMP:SGD.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IDA:UniProtKB.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006337; P:nucleosome disassembly; IMP:SGD.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IDA:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010468; P:regulation of gene expression; IMP:SGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IGI:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:SGD.
DR Gene3D; 2.60.40.1490; -; 1.
DR IDEAL; IID50170; -.
DR InterPro; IPR006818; ASF1-like.
DR InterPro; IPR036747; ASF1-like_sf.
DR InterPro; IPR017282; Hist_deposition_Asf1.
DR PANTHER; PTHR12040; PTHR12040; 1.
DR Pfam; PF04729; ASF1_hist_chap; 1.
DR PIRSF; PIRSF037759; Histone_Asf1; 1.
DR SUPFAM; SSF101546; SSF101546; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..279
FT /note="Histone chaperone ASF1"
FT /id="PRO_0000064695"
FT REGION 1..155
FT /note="Interaction with histone H3, histone H4, RAD53 and
FT the RF-C complex"
FT REGION 1..143
FT /note="Interaction with HIR1"
FT REGION 156..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..243
FT /evidence="ECO:0000255"
FT COMPBIAS 165..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 6
FT /note="L->M: Enhances transcriptional silencing."
FT /evidence="ECO:0000269|PubMed:17081973"
FT MUTAGEN 36..37
FT /note="HD->AA: Abrogates stimulation of replication-
FT independent chromatin assembly by the HIR complex and
FT abrogates telomeric silencing."
FT /evidence="ECO:0000269|PubMed:14680630,
FT ECO:0000269|PubMed:16303565"
FT MUTAGEN 37
FT /note="D->R: Reduces transcriptional silencing; when
FT associated with R-39."
FT /evidence="ECO:0000269|PubMed:15840725"
FT MUTAGEN 39
FT /note="E->R: Reduces transcriptional silencing; when
FT associated with R-37."
FT /evidence="ECO:0000269|PubMed:15840725"
FT MUTAGEN 45
FT /note="V->D: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to camptothecin."
FT /evidence="ECO:0000269|PubMed:16627621"
FT MUTAGEN 48
FT /note="S->R: Abrogates interaction with histone H3 and
FT histone H4 and enhances transcriptional silencing. Reduces
FT acetylation of histone H3 on 'K-9' and 'K-56'; when
FT associated with E-145 or E-147."
FT /evidence="ECO:0000269|PubMed:17081973,
FT ECO:0000269|PubMed:17107956"
FT MUTAGEN 53..54
FT /note="HD->AA: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to camptothecin."
FT /evidence="ECO:0000269|PubMed:16627621"
FT MUTAGEN 54
FT /note="D->R: Reduces transcriptional silencing."
FT /evidence="ECO:0000269|PubMed:15840725"
FT MUTAGEN 94
FT /note="V->D: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to bleomycin, camptothecin, HU and
FT MMS; when associated with D-96."
FT /evidence="ECO:0000269|PubMed:15840725,
FT ECO:0000269|PubMed:16627621, ECO:0000269|PubMed:17081973,
FT ECO:0000269|PubMed:17107956"
FT MUTAGEN 94
FT /note="V->R: Abrogates interaction with histone H3 and
FT histone H4, abrogates transcriptional silencing, reduces
FT acetylation of histone H3 on 'K-9' and 'K-56' and enhances
FT sensitivity to HU and MMS."
FT /evidence="ECO:0000269|PubMed:15840725,
FT ECO:0000269|PubMed:16627621, ECO:0000269|PubMed:17081973,
FT ECO:0000269|PubMed:17107956"
FT MUTAGEN 96
FT /note="L->D: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to bleomycin, camptothecin, HU and
FT MMS; when associated with D-94."
FT /evidence="ECO:0000269|PubMed:16627621"
FT MUTAGEN 105
FT /note="E->A: Decreases histone H3/H4 binding affinity."
FT /evidence="ECO:0000269|PubMed:31194870"
FT MUTAGEN 108
FT /note="R->E: Reduces transcriptional silencing."
FT /evidence="ECO:0000269|PubMed:15840725"
FT MUTAGEN 109
FT /note="V->M: Reduces interaction with histone H3 and
FT histone H4, enhances transcriptional silencing and reduces
FT transcriptional activation."
FT /evidence="ECO:0000269|PubMed:17081973"
FT MUTAGEN 112
FT /note="Y->A: Abrogates interaction with histone H3 and
FT histone H4 and enhances transcriptional silencing.
FT Abrogates transcriptional silencing, reduces
FT transcriptional activation, reduces acetylation of histone
FT H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and
FT MMS; when associated with E-145 or E-147."
FT /evidence="ECO:0000269|PubMed:16627621,
FT ECO:0000269|PubMed:17081973, ECO:0000269|PubMed:17107956"
FT MUTAGEN 112
FT /note="Y->E: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to bleomycin, camptothecin, HU and
FT MMS."
FT /evidence="ECO:0000269|PubMed:16627621,
FT ECO:0000269|PubMed:17081973, ECO:0000269|PubMed:17107956"
FT MUTAGEN 145
FT /note="R->A: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to bleomycin, camptothecin, HU and
FT MMS; when associated with A-147."
FT /evidence="ECO:0000269|PubMed:16627621,
FT ECO:0000269|PubMed:17081973, ECO:0000269|PubMed:17107956"
FT MUTAGEN 145
FT /note="R->E: Abrogates interaction with histone H3 and
FT histone H4, abrogates transcriptional silencing, reduces
FT transcriptional activation, reduces acetylation of histone
FT H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and
FT MMS; when associated with R-48; E-112 or E-147."
FT /evidence="ECO:0000269|PubMed:16627621,
FT ECO:0000269|PubMed:17081973, ECO:0000269|PubMed:17107956"
FT MUTAGEN 146
FT /note="V->L: Reduces interaction with histone H3 and
FT histone H4, enhances transcriptional silencing and reduces
FT transcriptional activation."
FT /evidence="ECO:0000269|PubMed:17081973"
FT MUTAGEN 147
FT /note="T->A: Reduces acetylation of histone H3 on 'K-56'
FT and enhances sensitivity to bleomycin, camptothecin, HU and
FT MMS; when associated with A-145."
FT /evidence="ECO:0000269|PubMed:16627621,
FT ECO:0000269|PubMed:17081973, ECO:0000269|PubMed:17107956"
FT MUTAGEN 147
FT /note="T->E: Enhances transcriptional silencing. Abrogates
FT interaction with histone H3 and histone H4, abrogates
FT transcriptional silencing, reduces transcriptional
FT activation, reduces acetylation of histone H3 on 'K-9' and
FT 'K-56' and enhances sensitivity to HU and MMS; when
FT associated with R-48; A-112 or E-145."
FT /evidence="ECO:0000269|PubMed:16627621,
FT ECO:0000269|PubMed:17081973, ECO:0000269|PubMed:17107956"
FT MUTAGEN 152
FT /note="V->VVFLHY: Impairs interaction with histone H3 and
FT RAD53 and enhances silencing at telomeres and mating-type
FT loci."
FT /evidence="ECO:0000269|PubMed:16582440"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6AYZ"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1ROC"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6F0Y"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2HUE"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:1ROC"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1ROC"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 104..119
FT /evidence="ECO:0007829|PDB:1ROC"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:1ROC"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1ROC"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1ROC"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2HUE"
SQ SEQUENCE 279 AA; 31603 MW; 186E76075C0B1644 CRC64;
MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS LDHDQELDSI
LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDEE
ELRENPPAKV QVDHIVRNIL AEKPRVTRFN IVWDNENEGD LYPPEQPGVD DEEEEDDEEE
DDDEDDEDDE DDDQEDGEGE AEEAAEEEEE EEEKTEDNET NLEEEEEDIE NSDGDEEEGE
EEVGSVDKNE DGNDKKRRKI EGGSTDIEST PKDAARSTN
