RT109_YEAST
ID RT109_YEAST Reviewed; 436 AA.
AC Q07794; D6VY01;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Histone acetyltransferase RTT109;
DE EC=2.3.1.48 {ECO:0000269|PubMed:17272722, ECO:0000269|PubMed:17369253, ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:21256037, ECO:0000269|PubMed:29300933, ECO:0000269|PubMed:31194870};
DE AltName: Full=Regulator of Ty1 transposition protein 109;
GN Name=RTT109 {ECO:0000303|PubMed:17046836};
GN Synonyms=KAT11 {ECO:0000303|PubMed:18568037}, KIM2, REM50;
GN OrderedLocusNames=YLL002W; ORFNames=L1377;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=11779788; DOI=10.1093/genetics/159.4.1449;
RA Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have
RT conserved roles in genome maintenance.";
RL Genetics 159:1449-1465(2001).
RN [5]
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 [6]
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 [7]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15282802; DOI=10.1002/yea.1133;
RA Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT "Localization of proteins that are coordinately expressed with Cln2 during
RT the cell cycle.";
RL Yeast 21:793-800(2004).
RN [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH VPS75.
RX PubMed=17369253; DOI=10.1074/jbc.m700611200;
RA Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.;
RT "The Rtt109-Vps75 histone acetyltransferase complex acetylates non-
RT nucleosomal histone H3.";
RL J. Biol. Chem. 282:14158-14164(2007).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ASF1 AND VPS75.
RX PubMed=17690098; DOI=10.1074/jbc.m702496200;
RA Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.;
RT "Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated
RT by ASF1 is required for replisome integrity.";
RL J. Biol. Chem. 282:28587-28596(2007).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH VPS75, AND INTERACTION WITH ASF1
RP AND VPS75.
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 [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17272722; DOI=10.1126/science.1135862;
RA Driscoll R., Hudson A., Jackson S.P.;
RT "Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine
RT 56.";
RL Science 315:649-652(2007).
RN [13]
RP FUNCTION, MUTAGENESIS OF ASP-89 AND 287-ASP-ASP-288, AND INTERACTION WITH
RP VPS75.
RX PubMed=17272723; DOI=10.1126/science.1133234;
RA Han J., Zhou H., Horazdovsky B., Zhang K., Xu R.-M., Zhang Z.;
RT "Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication.";
RL Science 315:653-655(2007).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP WITH HISTONE H3/H4 HETERODIMERS, AND DISRUPTION PHENOTYPE.
RX PubMed=19172748; DOI=10.1038/nsmb.1459;
RA Berndsen C.E., Tsubota T., Lindner S.E., Lee S., Holton J.M., Kaufman P.D.,
RA Keck J.L., Denu J.M.;
RT "Molecular functions of the histone acetyltransferase chaperone complex
RT Rtt109-Vps75.";
RL Nat. Struct. Mol. Biol. 15:948-956(2008).
RN [15]
RP FUNCTION.
RX PubMed=18577595; DOI=10.1073/pnas.0800057105;
RA Williams S.K., Truong D., Tyler J.K.;
RT "Acetylation in the globular core of histone H3 on lysine-56 promotes
RT chromatin disassembly during transcriptional activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9000-9005(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH VPS75.
RX PubMed=18723682; DOI=10.1073/pnas.0802393105;
RA Tang Y., Meeth K., Jiang E., Luo C., Marmorstein R.;
RT "Structure of Vps75 and implications for histone chaperone function.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12206-12211(2008).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
RN [18]
RP FUNCTION, BIOPHYSIOCHEMICAL PROPERTIES, IDENTIFICATION IN A COMPLEX WITH
RP VPS75, INTERACTION WITH VPS75, AND MUTAGENESIS OF ASP-287 AND ASP-288.
RX PubMed=20560668; DOI=10.1021/bi100381y;
RA Albaugh B.N., Kolonko E.M., Denu J.M.;
RT "Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone
RT complex.";
RL Biochemistry 49:6375-6385(2010).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [20] {ECO:0007744|PDB:3QM0}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-129 AND 180-436 IN COMPLEX WITH
RP ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, ACETYLATION AT LYS-290, AND MUTAGENESIS OF ASP-89;
RP TYR-199; TRP-222; ASP-287 AND LYS-290.
RX PubMed=18568037; DOI=10.1038/nsmb.1448;
RA Tang Y., Holbert M.A., Wurtele H., Meeth K., Rocha W., Gharib M., Jiang E.,
RA Thibault P., Verreault A., Cole P.A., Marmorstein R.;
RT "Fungal Rtt109 histone acetyltransferase is an unexpected structural
RT homolog of metazoan p300/CBP.";
RL Nat. Struct. Mol. Biol. 15:738-745(2008).
RN [21] {ECO:0007744|PDB:3CZ7}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-127 AND 171-403 IN COMPLEX WITH
RP ACETYL-COA, FUNCTION, IDENTIFICATION IN A COMPLEX WITH VPS75, INTERACTION
RP WITH VPS75, DISRUPTION PHENOTYPE, ACETYLATION AT LYS-290, AND MUTAGENESIS
RP OF GLU-66; PHE-84; PHE-285; ASP-287; ASP-288; LYS-290 AND TRP-312.
RX PubMed=18719104; DOI=10.1073/pnas.0805813105;
RA Stavropoulos P., Nagy V., Blobel G., Hoelz A.;
RT "Molecular basis for the autoregulation of the protein acetyl transferase
RT Rtt109.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12236-12241(2008).
RN [22] {ECO:0007744|PDB:2RIM, ECO:0007744|PDB:2ZFN}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ACETYL-COA, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, ACETYLATION AT LYS-290, AND MUTAGENESIS OF
RP ASP-89; ARG-194; HIS-211; TRP-221; ASP-288 AND LYS-290.
RX PubMed=18707894; DOI=10.1016/j.str.2008.07.006;
RA Lin C., Yuan Y.A.;
RT "Structural insights into histone H3 lysine 56 acetylation by Rtt109.";
RL Structure 16:1503-1510(2008).
RN [23] {ECO:0007744|PDB:3Q66, ECO:0007744|PDB:3Q68}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 1-426 IN COMPLEX WITH VPS75, AND
RP INTERACTION WITH VPS75 AND HISTONE H3/H4 HETERODIMERS.
RX PubMed=21454705; DOI=10.1074/jbc.c111.220715;
RA Su D., Hu Q., Zhou H., Thompson J.R., Xu R.M., Zhang Z., Mer G.;
RT "Structure and histone binding properties of the Vps75-Rtt109 chaperone-
RT lysine acetyltransferase complex.";
RL J. Biol. Chem. 286:15625-15629(2011).
RN [24] {ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-129; 134-165 AND 172-404 IN
RP COMPLEX WITH ACETYL-COA AND VPS75, FUNCTION, CATALYTIC ACTIVITY,
RP INTERACTION WITH VPS75, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-148;
RP 150-ILE-LEU-151; ARG-292; 355-ARG-LYS-356; 368-GLU--ASP-371; GLU-368;
RP GLU-374; 378-GLU--ASN-382 AND GLU-378.
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 [25] {ECO:0007744|PDB:6F0Y}
RP STRUCTURE BY NMR OF 419-433, FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION
RP WITH ASF1.
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 [26] {ECO:0007744|PDB:6O22}
RP STRUCTURE BY NMR IN COMPLEX WITH VPS75 AND ASF1, INTERACTION WITH ASF1 AND
RP VPS75, AND MUTAGENESIS OF 425-LYS--THR-436.
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-dependent acetylase that modifies 'Lys-9',
CC 'Lys-14', 'Lys-23', 'Lys-27', and 'Lys-56' on histone H3 (H3K9Ac,
CC H3K14Ac and H3K23Ac, H3K27Ac, and H3K56Ac) to promote nucleosome
CC assembly, genomic stability, DNA repair and transcriptional regulation
CC during mitotic S-phase (PubMed:31194870, PubMed:17046836,
CC PubMed:17369253, PubMed:17320445, PubMed:17272723, PubMed:18723682,
CC PubMed:20560668, PubMed:21256037, PubMed:29300933, PubMed:19172748,
CC PubMed:19683497). Its residue selectivity is influenced by the
CC acetylation status of histone H3, and also the presence of histone
CC chaperone ASF1 that shifts selectivity to 'Lys-56' when H3K14Ac is
CC already present (PubMed:31194870). H3K56 acetylation weakens the
CC interaction between the histone core and the surrounding DNA in the
CC nucleosomal particle and drives chromatin disassembly
CC (PubMed:18577595). Autoacetylates (PubMed:18568037, PubMed:18707894,
CC PubMed:18719104). Independently of acetyltransferase activity,
CC stimulates histone deposition by VPS75 (PubMed:19172748). Involved in
CC regulation of Ty1 transposition (PubMed:11779788).
CC {ECO:0000269|PubMed:11779788, ECO:0000269|PubMed:17046836,
CC ECO:0000269|PubMed:17272723, ECO:0000269|PubMed:17320445,
CC ECO:0000269|PubMed:17369253, ECO:0000269|PubMed:18568037,
CC ECO:0000269|PubMed:18577595, ECO:0000269|PubMed:18707894,
CC ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:18723682,
CC ECO:0000269|PubMed:19172748, ECO:0000269|PubMed:19683497,
CC ECO:0000269|PubMed:20560668, ECO:0000269|PubMed:21256037,
CC ECO:0000269|PubMed:29300933, ECO:0000269|PubMed:31194870}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:17272722, ECO:0000269|PubMed:17369253,
CC ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:18568037,
CC ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:19172748,
CC ECO:0000269|PubMed:21256037, ECO:0000269|PubMed:29300933,
CC ECO:0000269|PubMed:31194870};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000269|PubMed:17272722, ECO:0000269|PubMed:17369253,
CC ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:18568037,
CC ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:19172748,
CC ECO:0000269|PubMed:21256037, ECO:0000269|PubMed:29300933,
CC ECO:0000269|PubMed:31194870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894,
CC ECO:0000269|PubMed:18719104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894,
CC ECO:0000269|PubMed:18719104};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for acetyl-CoA (at pH 7.5, 25 degrees Celsius in the
CC presence of VPS75 chaperone) {ECO:0000269|PubMed:20560668};
CC KM=8 uM for acetyl-CoA (at pH 8, 30 degrees Celsius in the presence
CC of VPS75 chaperone) {ECO:0000269|PubMed:18568037};
CC KM=1.0 uM for acetyl-CoA (at pH 7.0, 25 degrees Celsius in the
CC presence of VPS75 chaperone) {ECO:0000269|PubMed:19172748};
CC KM=0.3 uM for acetyl-CoA (at pH 7.0, 25 degrees Celsius)
CC {ECO:0000269|PubMed:19172748};
CC KM=7 uM for histone H3 (at pH 7.5, 25 degrees Celsius in the presence
CC of VPS75 chaperone {ECO:0000269|PubMed:20560668};
CC KM=8.5 uM for histone H3 (at pH 8, 30 degrees Celsius in the presence
CC of VPS75 chaperone) {ECO:0000269|PubMed:18568037};
CC KM=8.1 uM for histone H3 (at pH 7.0, 25 degrees Celsius)
CC {ECO:0000269|PubMed:19172748};
CC KM=1.4 uM for histone H3/H4 (at pH 7.0, 25 degrees Celsius in the
CC presence of VPS75 chaperone) {ECO:0000269|PubMed:19172748};
CC KM=2.9 uM for histone H3/H4 (at pH 7.0, 25 degrees Celsius)
CC {ECO:0000269|PubMed:19172748};
CC Note=kcat is 0.11 sec(-1) with acetyl-CoA as substrate (at pH 7.5, 25
CC degrees Celsius in the presence of VPS75 chaperone)
CC (PubMed:20560668). kcat is 0.19 sec(-1) with acetyl-CoA as substrate
CC (at pH 7.0, 25 degrees Celsius in the presence of VPS75 chaperone)
CC (PubMed:19172748). kcat is 0.0017 sec(-1) with acetyl-CoA as
CC substrate (at pH 7.0, 25 degrees Celsius) (PubMed:19172748). kcat is
CC 0.62 sec(-1) with histone H3 as substrate (at pH 7.5, 25 degrees
CC Celsius in the presence of VPS75 chaperone (PubMed:20560668). kcat is
CC 22.5 min(-1) with histone H3 (at pH 8, 30 degrees Celsius in the
CC presence of VPS75 chaperone) (PubMed:18568037). kcat is 0.0033 sec(-
CC 1) with acetyl-CoA as substrate (at pH 7.0, 25 degrees Celsius)
CC (PubMed:19172748). kcat is 0.11 sec(-1) with histone H3/H4 as
CC substrate (at pH 7.0, 25 degrees Celsius in the presence of VPS75
CC chaperone) (PubMed:19172748). kcat is 0.0033 sec(-1) with histone
CC H3/H4 as substrate (at pH 7.0, 25 degrees Celsius) (PubMed:19172748).
CC {ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:19172748,
CC ECO:0000269|PubMed:20560668};
CC pH dependence:
CC Optimum pH is >8.5. {ECO:0000269|PubMed:20560668};
CC -!- SUBUNIT: Forms a complex composed of two RTT109 subunits and one VPS75
CC homodimer; each RTT109 subunit interacts predominantly with VPS75
CC instead of interacting with the other RTT109 subunit (PubMed:21256037,
CC PubMed:20560668, PubMed:17320445, PubMed:31387991, PubMed:18719104).
CC Interacts with VPS75; the interaction is direct (PubMed:31387991,
CC PubMed:20560668, PubMed:17369253, PubMed:17690098, PubMed:17320445,
CC PubMed:17272723, PubMed:18723682, PubMed:18719104, PubMed:21256037).
CC Interacts (via C-terminus) with ASF1; the interaction is direct
CC (PubMed:29300933, PubMed:31387991, PubMed:17690098, PubMed:17320445).
CC Interacts with histone H3/H4 heterodimers via histone H3
CC (PubMed:21454705, PubMed:19172748). {ECO:0000269|PubMed:17272723,
CC ECO:0000269|PubMed:17320445, ECO:0000269|PubMed:17369253,
CC ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:18719104,
CC ECO:0000269|PubMed:18723682, ECO:0000269|PubMed:19172748,
CC ECO:0000269|PubMed:20560668, ECO:0000269|PubMed:21256037,
CC ECO:0000269|PubMed:21454705, ECO:0000269|PubMed:29300933,
CC ECO:0000269|PubMed:31387991}.
CC -!- INTERACTION:
CC Q07794; P25293: NAP1; NbExp=2; IntAct=EBI-2887026, EBI-11850;
CC Q07794; P53853: VPS75; NbExp=20; IntAct=EBI-2887026, EBI-29225;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15282802}.
CC -!- INDUCTION: Expression peaks in cell cycle G1.
CC {ECO:0000269|PubMed:15282802}.
CC -!- DISRUPTION PHENOTYPE: Abolishes acetylation of histone H3 'Lys-56';
CC simultaneous disruption of GCN5 also abolishes acetylation of histone
CC H3 'Lys-9' and 'Lys-27' (PubMed:21256037). Decreases acetylation of
CC histone H3 'Lys-9' and 'Lys-23' (PubMed:19172748). Decreases HTA1 RNA
CC level; simultaneous disruption of HIR1 or RTT106 alleviates the effect
CC (PubMed:19683497). Increases sensitivity to methyl methane sulfonate,
CC hydroxyurea, and camptothecin (genotoxic stress) (PubMed:18568037,
CC PubMed:18719104). {ECO:0000269|PubMed:18568037,
CC ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:19172748,
CC ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:21256037}.
CC -!- MISCELLANEOUS: Present with 1140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RTT109 family. {ECO:0000305}.
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DR EMBL; X91488; CAA62768.1; -; Genomic_DNA.
DR EMBL; Z73107; CAA97445.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09317.1; -; Genomic_DNA.
DR PIR; S64744; S64744.
DR RefSeq; NP_013099.1; NM_001181822.1.
DR PDB; 2RIM; X-ray; 2.20 A; A=1-436.
DR PDB; 2ZFN; X-ray; 1.90 A; A=1-436.
DR PDB; 3CZ7; X-ray; 2.00 A; A=1-127, A=171-403.
DR PDB; 3Q33; X-ray; 2.80 A; A=1-436.
DR PDB; 3Q35; X-ray; 3.30 A; A=1-436.
DR PDB; 3Q66; X-ray; 2.70 A; C=1-436.
DR PDB; 3Q68; X-ray; 2.70 A; C=1-436.
DR PDB; 3QM0; X-ray; 3.10 A; A=1-436.
DR PDB; 6F0Y; NMR; -; B=419-433.
DR PDB; 6O22; Other; -; C=1-436.
DR PDBsum; 2RIM; -.
DR PDBsum; 2ZFN; -.
DR PDBsum; 3CZ7; -.
DR PDBsum; 3Q33; -.
DR PDBsum; 3Q35; -.
DR PDBsum; 3Q66; -.
DR PDBsum; 3Q68; -.
DR PDBsum; 3QM0; -.
DR PDBsum; 6F0Y; -.
DR PDBsum; 6O22; -.
DR AlphaFoldDB; Q07794; -.
DR SASBDB; Q07794; -.
DR SMR; Q07794; -.
DR BioGRID; 31249; 575.
DR ComplexPortal; CPX-1333; RTT109-VPS75 histone acetyltransferase complex.
DR DIP; DIP-8842N; -.
DR IntAct; Q07794; 4.
DR MINT; Q07794; -.
DR STRING; 4932.YLL002W; -.
DR ChEMBL; CHEMBL3414417; -.
DR PaxDb; Q07794; -.
DR PRIDE; Q07794; -.
DR EnsemblFungi; YLL002W_mRNA; YLL002W; YLL002W.
DR GeneID; 850658; -.
DR KEGG; sce:YLL002W; -.
DR SGD; S000003925; RTT109.
DR VEuPathDB; FungiDB:YLL002W; -.
DR eggNOG; KOG4534; Eukaryota.
DR GeneTree; ENSGT00940000176814; -.
DR HOGENOM; CLU_050421_0_0_1; -.
DR InParanoid; Q07794; -.
DR OMA; ADTNGYC; -.
DR BioCyc; YEAST:G3O-32107-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR EvolutionaryTrace; Q07794; -.
DR PRO; PR:Q07794; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07794; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0070775; C:H3 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:SGD.
DR GO; GO:0036408; F:histone acetyltransferase activity (H3-K14 specific); IDA:UniProtKB.
DR GO; GO:0043994; F:histone acetyltransferase activity (H3-K23 specific); IDA:UniProtKB.
DR GO; GO:0044017; F:histone acetyltransferase activity (H3-K27 specific); IDA:UniProtKB.
DR GO; GO:0032931; F:histone acetyltransferase activity (H3-K56 specific); IDA:UniProtKB.
DR GO; GO:0043992; F:histone acetyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0043972; P:histone H3-K23 acetylation; IDA:UniProtKB.
DR GO; GO:0043974; P:histone H3-K27 acetylation; IDA:UniProtKB.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IDA:UniProtKB.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IDA:UniProtKB.
DR GO; GO:0043007; P:maintenance of rDNA; IGI:SGD.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; IMP:UniProtKB.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR IDEAL; IID50225; -.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR016849; Rtt109.
DR PANTHER; PTHR31571:SF2; PTHR31571:SF2; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR PIRSF; PIRSF027124; Histone_acetylase_Rtt109; 1.
DR SMART; SM01250; KAT11; 1.
DR PROSITE; PS51728; RTT109_HAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA damage; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..436
FT /note="Histone acetyltransferase RTT109"
FT /id="PRO_0000268738"
FT DOMAIN 2..404
FT /note="Rtt109-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01064"
FT REGION 128..170
FT /note="Interaction with VPS75"
FT /evidence="ECO:0000269|PubMed:18719104,
FT ECO:0000269|PubMed:21256037, ECO:0000269|PubMed:21454705"
FT REGION 419..433
FT /note="Interaction with ASF1"
FT /evidence="ECO:0000269|PubMed:31387991"
FT ACT_SITE 288
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:18707894"
FT BINDING 88..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104,
FT ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN,
FT ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33,
FT ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0"
FT BINDING 97..101
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104,
FT ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN,
FT ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33,
FT ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0"
FT BINDING 192
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0007744|PDB:3QM0"
FT BINDING 196
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:21256037, ECO:0007744|PDB:3Q33,
FT ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0"
FT BINDING 211..213
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104,
FT ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN,
FT ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33,
FT ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0"
FT BINDING 221
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18707894,
FT ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:21256037,
FT ECO:0007744|PDB:2ZFN, ECO:0007744|PDB:3CZ7,
FT ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35"
FT MOD_RES 290
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104"
FT MUTAGEN 66
FT /note="E->A: Mildly increases sensitivity to methyl methane
FT sulfonate, camptothecin and hydroxyurea (genotoxic
FT stress)."
FT /evidence="ECO:0000269|PubMed:18719104"
FT MUTAGEN 84
FT /note="F->A: Increases sensitivity to methyl methane
FT sulfonate, camptothecin and hydroxyurea (genotoxic
FT stress)."
FT /evidence="ECO:0000269|PubMed:18719104"
FT MUTAGEN 89
FT /note="D->A: Abolishes histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:17272723,
FT ECO:0000269|PubMed:18707894"
FT MUTAGEN 89
FT /note="D->N: Decreases histone acetylase activity.
FT Decreases expression (at protein level). Increases
FT sensitivity to methyl methane sulfonate and hydroxyurea
FT (genotoxic stress)."
FT /evidence="ECO:0000269|PubMed:18568037"
FT MUTAGEN 148
FT /note="L->D: Decreases binding and activity stimulation by
FT VPS75. Decreases acetylation of histone H3 'Lys-9' and
FT 'Lys-27'."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 150..151
FT /note="IL->DD: Decreases binding and activity stimulation
FT by VPS75."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 194
FT /note="R->A,E: Decreases histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:18707894,
FT ECO:0000269|PubMed:21256037"
FT MUTAGEN 199
FT /note="Y->S: Decreases histone acetylase activity.
FT Increases sensitivity to methyl methane sulfonate and
FT hydroxyurea (genotoxic stress)."
FT /evidence="ECO:0000269|PubMed:18568037"
FT MUTAGEN 211
FT /note="H->A: Decreases histone acetylase activity; when
FT associated with A-222."
FT /evidence="ECO:0000269|PubMed:18707894"
FT MUTAGEN 221
FT /note="W->A: Decreases histone acetylase activity; when
FT associated with A-211."
FT /evidence="ECO:0000269|PubMed:18707894"
FT MUTAGEN 222
FT /note="W->F: Decreases histone acetylase activity.
FT Increases sensitivity to methyl methane sulfonate and
FT hydroxyurea (genotoxic stress)."
FT /evidence="ECO:0000269|PubMed:18568037"
FT MUTAGEN 285
FT /note="F->A: Increases sensitivity to methyl methane
FT sulfonate, camptothecin and hydroxyurea (genotoxic
FT stress)."
FT /evidence="ECO:0000269|PubMed:18719104"
FT MUTAGEN 287..288
FT /note="DD->AA,NN: Decreases histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:17272723,
FT ECO:0000269|PubMed:20560668"
FT MUTAGEN 287
FT /note="D->A,N: Decreases histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:20560668"
FT MUTAGEN 287
FT /note="D->A: Increases sensitivity to methyl methane
FT sulfonate, camptothecin and hydroxyurea (genotoxic
FT stress)."
FT /evidence="ECO:0000269|PubMed:18719104"
FT MUTAGEN 288
FT /note="D->A: Abolishes histone acetylase activity.
FT Increases sensitivity to methyl methane sulfonate,
FT camptothecin and hydroxyurea (genotoxic stress)."
FT /evidence="ECO:0000269|PubMed:18707894,
FT ECO:0000269|PubMed:18719104"
FT MUTAGEN 288
FT /note="D->N: Decreases histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:20560668"
FT MUTAGEN 290
FT /note="K->A: Abolishes histone acetylase activity.
FT Increases sensitivity to methyl methane sulfonate,
FT camptothecin and hydroxyurea (genotoxic stress)."
FT /evidence="ECO:0000269|PubMed:18707894,
FT ECO:0000269|PubMed:18719104"
FT MUTAGEN 290
FT /note="K->E,W: Increases sensitivity to methyl methane
FT sulfonate, camptothecin and hydroxyurea (genotoxic
FT stress)."
FT /evidence="ECO:0000269|PubMed:18719104"
FT MUTAGEN 290
FT /note="K->R: Normal histone acetylase activity. Increases
FT sensitivity to methyl methane sulfonate, camptothecin and
FT hydroxyurea (genotoxic stress)."
FT /evidence="ECO:0000269|PubMed:18568037,
FT ECO:0000269|PubMed:18719104"
FT MUTAGEN 292
FT /note="R->E: Decreases activity stimulation by ASF1."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 312
FT /note="W->A: Increases sensitivity to methyl methane
FT sulfonate, camptothecin and hydroxyurea (genotoxic
FT stress)."
FT /evidence="ECO:0000269|PubMed:18719104"
FT MUTAGEN 355..356
FT /note="RK->EE: Decreases binding and activity stimulation
FT by VPS75."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 368..371
FT /note="EEYD->RRYR: Decreases histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 368
FT /note="E->R: Decreases histone acetylase activity."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 374
FT /note="E->R: Decreases activity stimulation by VPS75."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 378..382
FT /note="EAFTN->RAFTR: Decreases binding and activity
FT stimulation by VPS75. Decreases acetylation of histone H3
FT 'Lys-9' and 'Lys-27'."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 378
FT /note="E->R: Decreases activity stimulation by VPS75."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 425..436
FT /note="Missing: Abolishes ASF1 binding."
FT /evidence="ECO:0000269|PubMed:31387991"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3Q68"
FT STRAND 44..57
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 60..77
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:3Q66"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3Q66"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3Q66"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3Q66"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3Q66"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3QM0"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3Q66"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3QM0"
FT HELIX 215..233
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3Q68"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3CZ7"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:2ZFN"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:2ZFN"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:3Q66"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2ZFN"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 373..391
FT /evidence="ECO:0007829|PDB:2ZFN"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:2ZFN"
FT HELIX 411..423
FT /evidence="ECO:0007829|PDB:3Q66"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:6F0Y"
SQ SEQUENCE 436 AA; 50096 MW; 17825D6EF97C4BB5 CRC64;
MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK
VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL
QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR FQQDLYLSFT
CPREILTKIC LFTRPASQYL FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA
KLRIPGEDPA RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE
DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI VPKSRKQFRA
IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG KREHRERNQP VPASNINTLA
ITMLKPRKKA KALPKT
