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 27-MAR-2024, entry version 171. 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 uM for acetyl-CoA (at pH 7.0, 25 degrees Celsius in the presence CC 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 CC is 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 CC sec(-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}. 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; 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; 597. 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 iPTMnet; Q07794; -. DR PaxDb; 4932-YLL002W; -. DR PeptideAtlas; Q07794; -. DR EnsemblFungi; YLL002W_mRNA; YLL002W; YLL002W. DR GeneID; 850658; -. DR KEGG; sce:YLL002W; -. DR AGR; SGD:S000003925; -. 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; FLEHLIV; -. DR OrthoDB; 2787984at2759; -. DR BioCyc; YEAST:G3O-32107-MONOMER; -. DR BRENDA; 2.3.1.48; 984. DR BioGRID-ORCS; 850658; 0 hits in 10 CRISPR screens. 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:histone H3 acetyltransferase activity; IDA:SGD. DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043994; F:histone H3K23 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0032931; F:histone H3K56 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043992; F:histone H3K9 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IMP:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central. DR GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; IEA:InterPro. DR GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB. 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: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:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD. DR GO; GO:0010526; P:retrotransposon silencing; IMP:SGD. DR IDEAL; IID50225; -. DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP. DR InterPro; IPR016849; Rtt109. DR PANTHER; PTHR31571; ALTERED INHERITANCE OF MITOCHONDRIA PROTEIN 6; 1. DR PANTHER; PTHR31571:SF2; HISTONE ACETYLTRANSFERASE RTT109; 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 //