RPA34_YEAST
ID RPA34_YEAST Reviewed; 233 AA.
AC P47006; D6VW37;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA34;
DE Short=A34;
DE AltName: Full=DNA-directed DNA-dependent RNA polymerase 34.5 kDa polypeptide;
DE Short=A34.5;
GN Name=RPA34; OrderedLocusNames=YJL148W; ORFNames=J0637;
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 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [2]
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 [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, IDENTIFICATION IN THE RNA POL I COMPLEX, AND PHOSPHORYLATION.
RX PubMed=9121426; DOI=10.1128/mcb.17.4.1787;
RA Gadal O., Mariotte-Labarre S., Chedin S., Quemeneur E., Carles C.,
RA Sentenac A., Thuriaux P.;
RT "A34.5, a nonessential component of yeast RNA polymerase I, cooperates with
RT subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis
RT machine.";
RL Mol. Cell. Biol. 17:1787-1795(1997).
RN [5]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-60, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14, AND
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 [9]
RP FUNCTION, INTERACTION WITH RPA49, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBUNIT.
RX PubMed=20797630; DOI=10.1016/j.molcel.2010.07.028;
RA Geiger S.R., Lorenzen K., Schreieck A., Hanecker P., Kostrewa D.,
RA Heck A.J., Cramer P.;
RT "RNA polymerase I contains a TFIIF-related DNA-binding subcomplex.";
RL Mol. Cell 39:583-594(2010).
RN [10]
RP ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
RX PubMed=12145213; DOI=10.1093/emboj/cdf392;
RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V.,
RA Schultz P.;
RT "Localization of the yeast RNA polymerase I-specific subunits.";
RL EMBO J. 21:4136-4144(2002).
RN [11]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11918799; DOI=10.1046/j.1365-2958.2002.02824.x;
RA Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.;
RT "Rpa12p, a conserved RNA polymerase I subunit with two functional
RT domains.";
RL Mol. Microbiol. 43:1105-1113(2002).
RN [12]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [13]
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 [14]
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 [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA
CC precursors. Besides, RNA polymerase I has intrinsic RNA cleavage
CC activity. The heterodimer formed by RPA34 and RPA49 stimulates
CC transcript elongation by Pol I. {ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:20797630, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184, ECO:0000269|PubMed:9121426}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of
CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5,
CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and
CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43
CC form the stalk that mediates interactions with transcription initiation
CC factors and newly synthesized RNA. Forms a TFIIF-like heterodimer with
CC RPA49; the heterodimer formed by RPA34 and RPA49 can be dissociated
CC from the Pol I core giving rise to a 12 subunit form A* of Pol I
CC (formerly called pol A) that shows impaired transcript elongation
CC activity and increased sensitivity to alpha-amanitin. The heterodimer
CC formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates
CC RPA12-dependent RNA cleavage. {ECO:0000269|PubMed:11717393,
CC ECO:0000269|PubMed:11918799, ECO:0000269|PubMed:12407181,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:20797630,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184,
CC ECO:0000269|PubMed:9121426}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA34 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; Z49423; CAA89443.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60807.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08653.1; -; Genomic_DNA.
DR PIR; S55165; S55165.
DR RefSeq; NP_012387.1; NM_001181581.1.
DR PDB; 4C2M; X-ray; 2.80 A; 3/N=1-233.
DR PDB; 4C3H; X-ray; 3.27 A; N=1-233.
DR PDB; 4C3I; X-ray; 3.00 A; N=1-233.
DR PDB; 4C3J; X-ray; 3.35 A; N=1-233.
DR PDB; 4YM7; X-ray; 5.50 A; AN/BN/CN/DN/EN/FN=1-233.
DR PDB; 5G5L; EM; 4.80 A; N=1-233.
DR PDB; 5LMX; EM; 4.90 A; N=1-233.
DR PDB; 5M3F; EM; 3.80 A; N=1-233.
DR PDB; 5M3M; EM; 4.00 A; N=1-233.
DR PDB; 5M5W; EM; 3.80 A; N=1-233.
DR PDB; 5M5X; EM; 4.00 A; N=1-233.
DR PDB; 5M5Y; EM; 4.00 A; N=1-233.
DR PDB; 5M64; EM; 4.60 A; N=1-233.
DR PDB; 5N5Y; EM; 7.70 A; N=1-233.
DR PDB; 5N5Z; EM; 7.70 A; N=1-233.
DR PDB; 5N60; EM; 7.70 A; N=1-233.
DR PDB; 5N61; EM; 3.40 A; N=1-233.
DR PDB; 5OA1; EM; 4.40 A; N=1-233.
DR PDB; 5W5Y; EM; 3.80 A; N=1-233.
DR PDB; 5W64; EM; 4.20 A; N=1-233.
DR PDB; 5W65; EM; 4.30 A; N=1-233.
DR PDB; 5W66; EM; 3.90 A; N=1-233.
DR PDB; 6H67; EM; 3.60 A; N=1-233.
DR PDB; 6H68; EM; 4.60 A; N=1-233.
DR PDB; 6HKO; EM; 3.42 A; N=1-233.
DR PDB; 6RQH; EM; 3.70 A; N=1-233.
DR PDB; 6RQL; EM; 2.90 A; N=1-233.
DR PDB; 6RQT; EM; 4.00 A; N=1-233.
DR PDB; 6RRD; EM; 3.10 A; N=1-233.
DR PDB; 6RUI; EM; 2.70 A; N=1-233.
DR PDB; 6RUO; EM; 3.50 A; N=1-233.
DR PDB; 6RWE; EM; 3.00 A; N=1-233.
DR PDB; 6TPS; EM; 3.54 A; N=1-233.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; P47006; -.
DR SMR; P47006; -.
DR BioGRID; 33610; 544.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-7973N; -.
DR IntAct; P47006; 29.
DR MINT; P47006; -.
DR STRING; 4932.YJL148W; -.
DR iPTMnet; P47006; -.
DR MaxQB; P47006; -.
DR PaxDb; P47006; -.
DR PRIDE; P47006; -.
DR EnsemblFungi; YJL148W_mRNA; YJL148W; YJL148W.
DR GeneID; 853293; -.
DR KEGG; sce:YJL148W; -.
DR SGD; S000003684; RPA34.
DR VEuPathDB; FungiDB:YJL148W; -.
DR eggNOG; ENOG502S2EI; Eukaryota.
DR HOGENOM; CLU_090034_0_0_1; -.
DR InParanoid; P47006; -.
DR OMA; HFPTGYG; -.
DR BioCyc; YEAST:G3O-31592-MON; -.
DR PRO; PR:P47006; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47006; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:SGD.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR InterPro; IPR013240; DNA-dir_RNA_pol1_su_RPA34.
DR Pfam; PF08208; RNA_polI_A34; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Transcription.
FT CHAIN 1..233
FT /note="DNA-directed RNA polymerase I subunit RPA34"
FT /id="PRO_0000203031"
FT REGION 179..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..233
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6RRD"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4C2M"
SQ SEQUENCE 233 AA; 26875 MW; DCD42DFEC574EDB6 CRC64;
MSKLSKDYVS DSDSDDEVIS NEFSIPDGFK KCKHLKNFPL NGDNKKKAKQ QQVWLIKFPS
NVDISKLKSL PVDFESSTTM TIDKHDYKIM DDTDIESSLT QDNLSNMTLL VPSESKESLK
IASTAKDNAP LQFDKVFSVS ETAKIPAIDY SKVRVPRKDV PKVEGLKLEH FATGYDAEDF
HVAEEVKENK KEPKKRSHHD DEEESSEKKK KKKEKREKRE KKDKKDKKKK HRD
