RSC58_YEAST
ID RSC58_YEAST Reviewed; 502 AA.
AC Q07979; D6VY35;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Chromatin structure-remodeling complex protein RSC58;
DE AltName: Full=Remodel the structure of chromatin complex subunit 58;
GN Name=RSC58; OrderedLocusNames=YLR033W;
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] {ECO:0000305}
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 [2]
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 [3] {ECO:0000305}
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=8980231; DOI=10.1016/s0092-8674(00)81820-6;
RA Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H.,
RA Tempst P., Du J., Laurent B.C., Kornberg R.D.;
RT "RSC, an essential, abundant chromatin-remodeling complex.";
RL Cell 87:1249-1260(1996).
RN [4] {ECO:0000305}
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=10025404; DOI=10.1016/s0092-8674(00)80551-6;
RA Lorch Y., Zhang M., Kornberg R.D.;
RT "Histone octamer transfer by a chromatin-remodeling complex.";
RL Cell 96:389-392(1999).
RN [5] {ECO:0000305}
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=10329629; DOI=10.1093/emboj/18.10.2836;
RA Moreira J.M.A., Holmberg S.;
RT "Transcriptional repression of the yeast CHA1 gene requires the chromatin-
RT remodeling complex RSC.";
RL EMBO J. 18:2836-2844(1999).
RN [6] {ECO:0000305}
RP COMPOSITION OF THE RSC COMPLEX.
RX PubMed=10619019; DOI=10.1016/s1097-2765(00)80382-2;
RA Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D.,
RA Winston F.;
RT "Two functionally distinct forms of the RSC nucleosome-remodeling complex,
RT containing essential AT hook, BAH, and bromodomains.";
RL Mol. Cell 4:715-723(1999).
RN [7] {ECO:0000305}
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=12183366; DOI=10.1101/gad.995002;
RA Saha A., Wittmeyer J., Cairns B.R.;
RT "Chromatin remodeling by RSC involves ATP-dependent DNA translocation.";
RL Genes Dev. 16:2120-2134(2002).
RN [8] {ECO:0000305}
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=12072455; DOI=10.1093/genetics/161.2.575;
RA Chai B., Hsu J.-M., Du J., Laurent B.C.;
RT "Yeast RSC function is required for organization of the cellular
RT cytoskeleton via an alternative PKC1 pathway.";
RL Genetics 161:575-584(2002).
RN [9] {ECO:0000305}
RP IDENTIFICATION IN THE RSC COMPLEX.
RX PubMed=12052880; DOI=10.1128/mcb.22.13.4723-4738.2002;
RA Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.;
RT "Proteomics of the eukaryotic transcription machinery: identification of
RT proteins associated with components of yeast TFIID by multidimensional mass
RT spectrometry.";
RL Mol. Cell. Biol. 22:4723-4738(2002).
RN [10] {ECO:0000305}
RP FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION OF THE
RP RSC COMPLEX WITH HISTONES.
RX PubMed=12697820; DOI=10.1128/mcb.23.9.3202-3215.2003;
RA Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.;
RT "The yeast RSC chromatin-remodeling complex is required for kinetochore
RT function in chromosome segregation.";
RL Mol. Cell. Biol. 23:3202-3215(2003).
RN [11]
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).
CC -!- FUNCTION: Component of the chromatin structure-remodeling complex
CC (RSC), which is involved in transcription regulation and nucleosome
CC positioning. RSC is responsible for the transfer of a histone octamer
CC from a nucleosome core particle to naked DNA. The reaction requires ATP
CC and involves an activated RSC-nucleosome intermediate. Remodeling
CC reaction also involves DNA translocation, DNA twist and conformational
CC change. As a reconfigurer of centromeric and flanking nucleosomes, RSC
CC complex is required both for proper kinetochore function in chromosome
CC segregation and, via a PKC1-dependent signaling pathway, for
CC organization of the cellular cytoskeleton.
CC {ECO:0000269|PubMed:10025404, ECO:0000269|PubMed:10329629,
CC ECO:0000269|PubMed:12072455, ECO:0000269|PubMed:12183366,
CC ECO:0000269|PubMed:12697820, ECO:0000269|PubMed:8980231}.
CC -!- SUBUNIT: Component of the two forms of the RSC complex composed of at
CC least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30,
CC RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102.
CC The complexes interact with histone and histone variant components of
CC centromeric chromatin. {ECO:0000269|PubMed:12052880}.
CC -!- INTERACTION:
CC Q07979; P25632: RSC6; NbExp=7; IntAct=EBI-36549, EBI-21941;
CC Q07979; P32597: STH1; NbExp=6; IntAct=EBI-36549, EBI-18410;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12697820}.
CC Note=Localizes to centromeric and flanking chromatin. Association with
CC these loci is dependent on STH1.
CC -!- MISCELLANEOUS: Present with 4460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z73205; CAA97557.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09351.1; -; Genomic_DNA.
DR PIR; S64860; S64860.
DR RefSeq; NP_013133.1; NM_001181920.1.
DR PDB; 6K15; EM; 3.40 A; A=1-502.
DR PDB; 6KW3; EM; 7.13 A; A=1-502.
DR PDB; 6KW4; EM; 7.55 A; A=1-502.
DR PDB; 6KW5; EM; 10.13 A; A=1-502.
DR PDB; 6TDA; EM; 15.00 A; P=1-502.
DR PDB; 6V8O; EM; 3.07 A; O=1-502.
DR PDB; 6V92; EM; 20.00 A; O=1-502.
DR PDBsum; 6K15; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR AlphaFoldDB; Q07979; -.
DR SMR; Q07979; -.
DR BioGRID; 31307; 262.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-6656N; -.
DR IntAct; Q07979; 104.
DR MINT; Q07979; -.
DR STRING; 4932.YLR033W; -.
DR iPTMnet; Q07979; -.
DR MaxQB; Q07979; -.
DR PaxDb; Q07979; -.
DR PRIDE; Q07979; -.
DR EnsemblFungi; YLR033W_mRNA; YLR033W; YLR033W.
DR GeneID; 850720; -.
DR KEGG; sce:YLR033W; -.
DR SGD; S000004023; RSC58.
DR VEuPathDB; FungiDB:YLR033W; -.
DR eggNOG; ENOG502QQT5; Eukaryota.
DR HOGENOM; CLU_043834_0_0_1; -.
DR InParanoid; Q07979; -.
DR OMA; PNWYSLP; -.
DR BioCyc; YEAST:G3O-32192-MON; -.
DR PRO; PR:Q07979; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07979; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR Pfam; PF00439; Bromodomain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..502
FT /note="Chromatin structure-remodeling complex protein
FT RSC58"
FT /id="PRO_0000097473"
FT REGION 336..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 115..137
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 180..190
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:6K15"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 404..411
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 416..435
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 443..461
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:6K15"
SQ SEQUENCE 502 AA; 57794 MW; 8F8D01184DAE1F6F CRC64;
MTESVGGNKL VDFLVNVQSI LNAASVKCHV VDESFPAKFF EKNPDKIYES YCKFIKNRSN
SEGLIRNEDK LVLTTINKRF ENGEYEPIQG GFYKLYHDIK LVCTILIHFY PQGTRNYQLV
DKFYKFSSEL LLRECCRIGI ALTQTNNIKS RSGKLLSGNE MDEYDDDDAT ELDKIISYDF
IKISMNYTVP ISQTYQIRTK DMDLFSSIIS KSNLDKRPHE LPNTNFKINN VLPQTDIENE
APRLGFVGAN TSNIPDPTLP PTEMMTRFLH PNWYALPTTV WLKYGNYNSW APSFNENGTV
VDSTTRGLIW LERIGYMDLY EKNEKKVKQE ELLNTNEEGI NRKQNDENNK NVDGKSNGVQ
DDGGDNDNDA TIASANSEST ENKEQFIIKL QNLYNWTPSN YIGDDEIENF RNGTPDKLVS
DSLLKLKRLR KERILNKVLK PTTEERELYF KVKRILKEVI LAKKVSKVPI NNVRAFPVLQ
TNYNGSIPVV RAQPGRKRKH KK
