MED22_YEAST
ID MED22_YEAST Reviewed; 121 AA.
AC P32570; D6VQP9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 22;
DE AltName: Full=Mediator complex subunit 22;
DE AltName: Full=Suppressor of RNA polymerase B 6;
GN Name=SRB6; Synonyms=MED22; OrderedLocusNames=YBR253W; ORFNames=YBR1721;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ASN-86.
RC STRAIN=Z28;
RX PubMed=8324825; DOI=10.1016/0092-8674(93)90362-t;
RA Thompson C.M., Koleske A.J., Chao D.M., Young R.A.;
RT "A multisubunit complex associated with the RNA polymerase II CTD and TATA-
RT binding protein in yeast.";
RL Cell 73:1361-1375(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=8187178; DOI=10.1016/0092-8674(94)90221-6;
RA Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D.;
RT "A multiprotein mediator of transcriptional activation and its interaction
RT with the C-terminal repeat domain of RNA polymerase II.";
RL Cell 77:599-608(1994).
RN [6]
RP INTERACTION WITH SRB4.
RX PubMed=9660972; DOI=10.1016/s1097-2765(00)80088-x;
RA Koh S.S., Ansari A.Z., Ptashne M., Young R.A.;
RT "An activator target in the RNA polymerase II holoenzyme.";
RL Mol. Cell 1:895-904(1998).
RN [7]
RP INTERACTION WITH SRB4.
RX PubMed=9671455; DOI=10.1128/mcb.18.8.4455;
RA Lee T.I., Wyrick J.J., Koh S.S., Jennings E.G., Gadbois E.L., Young R.A.;
RT "Interplay of positive and negative regulators in transcription initiation
RT by RNA polymerase II holoenzyme.";
RL Mol. Cell. Biol. 18:4455-4462(1998).
RN [8]
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 [9]
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 [10]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=14623974; DOI=10.1073/pnas.2036346100;
RA Kuras L., Borggrefe T., Kornberg R.D.;
RT "Association of the Mediator complex with enhancers of active genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13887-13891(2003).
RN [11]
RP NOMENCLATURE.
RX PubMed=15175151; DOI=10.1016/j.molcel.2004.05.011;
RA Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J.,
RA Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M.,
RA Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P.,
RA Fukasawa T., Gustafsson C.M., Han M., He X., Herman P.K., Hinnebusch A.G.,
RA Holmberg S., Holstege F.C.P., Jaehning J.A., Kim Y.-J., Kuras L., Leutz A.,
RA Lis J.T., Meisterernest M., Naeaer A.M., Nasmyth K., Parvin J.D.,
RA Ptashne M., Reinberg D., Ronne H., Sadowski I., Sakurai H., Sipiczki M.,
RA Sternberg P.W., Stillman D.J., Strich R., Struhl K., Svejstrup J.Q.,
RA Tuck S., Winston F., Roeder R.G., Kornberg R.D.;
RT "A unified nomenclature for protein subunits of mediator complexes linking
RT transcriptional regulators to RNA polymerase II.";
RL Mol. Cell 14:553-557(2004).
RN [12]
RP TOPOLOGY OF THE MEDIATOR COMPLEX.
RX PubMed=15477388; DOI=10.1093/nar/gkh878;
RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
RT "A high resolution protein interaction map of the yeast Mediator complex.";
RL Nucleic Acids Res. 32:5379-5391(2004).
RN [13]
RP CHARACTERIZATION OF THE MEDIATOR COMPLEX.
RX PubMed=16002404; DOI=10.1074/jbc.c500150200;
RA Takagi Y., Chadick J.Z., Davis J.A., Asturias F.J.;
RT "Preponderance of free mediator in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:31200-31207(2005).
RN [14]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16076843; DOI=10.1074/jbc.m506067200;
RA Nair D., Kim Y., Myers L.C.;
RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription
RT in yeast extracts.";
RL J. Biol. Chem. 280:33739-33748(2005).
RN [15]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16263706; DOI=10.1074/jbc.m508253200;
RA Takagi Y., Kornberg R.D.;
RT "Mediator as a general transcription factor.";
RL J. Biol. Chem. 281:80-89(2006).
RN [16]
RP CHARACTERIZATION OF THE MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR
RP COMPLEX WITH RNA POLYMERASE II.
RX PubMed=17192271; DOI=10.1074/jbc.m609484200;
RA Baidoobonso S.M., Guidi B.W., Myers L.C.;
RT "Med19(Rox3) regulates intermodule interactions in the Saccharomyces
RT cerevisiae mediator complex.";
RL J. Biol. Chem. 282:5551-5559(2007).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.
RX PubMed=12191485; DOI=10.1016/s1097-2765(02)00598-1;
RA Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.;
RT "Structure of the yeast RNA polymerase II holoenzyme: mediator conformation
RT and polymerase interaction.";
RL Mol. Cell 10:409-415(2002).
RN [19]
RP INTERACTION WITH SRB4, FUNCTION OF THE MEDIATOR COMPLEX HEAD MODULE,
RP ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX HEAD MODULE, AND INTERACTION OF
RP THE MEDIATOR COMPLEX HEAD MODULE WITH RNA POLYMERASE II AND TFIIF.
RX PubMed=16885025; DOI=10.1016/j.molcel.2006.06.007;
RA Takagi Y., Calero G., Komori H., Brown J.A., Ehrensberger A.H., Hudmon A.,
RA Asturias F.J., Kornberg R.D.;
RT "Head module control of mediator interactions.";
RL Mol. Cell 23:355-364(2006).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. The Mediator complex, having a compact
CC conformation in its free form, is recruited to promoters by direct
CC interactions with regulatory proteins and serves for the assembly of a
CC functional preinitiation complex with RNA polymerase II and the general
CC transcription factors. The Mediator complex unfolds to an extended
CC conformation and partially surrounds RNA polymerase II, specifically
CC interacting with the unphosphorylated form of the C-terminal domain
CC (CTD) of RNA polymerase II. The Mediator complex dissociates from the
CC RNA polymerase II holoenzyme and stays at the promoter when
CC transcriptional elongation begins. {ECO:0000269|PubMed:16076843,
CC ECO:0000269|PubMed:16263706, ECO:0000269|PubMed:16885025}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of at
CC least 21 subunits that form three structurally distinct submodules. The
CC Mediator head module contains MED6, MED8, MED11, SRB4/MED17,
CC SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module
CC contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21
CC and SOH1/MED31, and the tail module contains MED2, PGD1/MED3,
CC RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules
CC interact directly with RNA polymerase II, whereas the elongated tail
CC module interacts with gene-specific regulatory proteins. SRB6/MED22
CC interacts directly with SRB4/MED17. {ECO:0000269|PubMed:16885025,
CC ECO:0000269|PubMed:17192271, ECO:0000269|PubMed:9660972,
CC ECO:0000269|PubMed:9671455}.
CC -!- INTERACTION:
CC P32570; Q99278: MED11; NbExp=17; IntAct=EBI-18039, EBI-27213;
CC P32570; P32569: SRB4; NbExp=11; IntAct=EBI-18039, EBI-18025;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2181 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 22 family.
CC {ECO:0000305}.
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DR EMBL; L12027; AAB08013.1; -; Genomic_DNA.
DR EMBL; X70529; CAA49917.1; -; Genomic_DNA.
DR EMBL; Z36122; CAA85216.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07369.1; -; Genomic_DNA.
DR PIR; S32956; S32956.
DR RefSeq; NP_009812.1; NM_001178601.1.
DR PDB; 3J1O; EM; 16.00 A; K=1-121.
DR PDB; 3R84; X-ray; 2.05 A; B/D/F/H/J/L/N/P/R/T/V/X=2-89.
DR PDB; 3RJ1; X-ray; 4.30 A; D/K/R=1-121.
DR PDB; 4GWP; X-ray; 4.20 A; D=1-121.
DR PDB; 4GWQ; X-ray; 4.50 A; D=1-121.
DR PDB; 4H62; X-ray; 3.00 A; V=96-121.
DR PDB; 4V1O; EM; 9.70 A; Z=2-121.
DR PDB; 5OQM; EM; 5.80 A; g=1-121.
DR PDB; 5SVA; EM; 15.30 A; S=1-121.
DR PDBsum; 3J1O; -.
DR PDBsum; 3R84; -.
DR PDBsum; 3RJ1; -.
DR PDBsum; 4GWP; -.
DR PDBsum; 4GWQ; -.
DR PDBsum; 4H62; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR AlphaFoldDB; P32570; -.
DR SMR; P32570; -.
DR BioGRID; 32948; 205.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-1433N; -.
DR IntAct; P32570; 55.
DR MINT; P32570; -.
DR STRING; 4932.YBR253W; -.
DR iPTMnet; P32570; -.
DR MaxQB; P32570; -.
DR PaxDb; P32570; -.
DR PRIDE; P32570; -.
DR EnsemblFungi; YBR253W_mRNA; YBR253W; YBR253W.
DR GeneID; 852555; -.
DR KEGG; sce:YBR253W; -.
DR SGD; S000000457; SRB6.
DR VEuPathDB; FungiDB:YBR253W; -.
DR eggNOG; ENOG502S77A; Eukaryota.
DR HOGENOM; CLU_130571_0_0_1; -.
DR InParanoid; P32570; -.
DR OMA; WLLTQIP; -.
DR BioCyc; YEAST:G3O-29178-MON; -.
DR PRO; PR:P32570; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32570; protein.
DR GO; GO:0070847; C:core mediator complex; IDA:SGD.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:ComplexPortal.
DR InterPro; IPR009332; Med22.
DR InterPro; IPR016530; Med22_Saccharomyce.
DR Pfam; PF06179; Med22; 1.
DR PIRSF; PIRSF007936; SRB6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..121
FT /note="Mediator of RNA polymerase II transcription subunit
FT 22"
FT /id="PRO_0000096379"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 86
FT /note="N->K: In SRB6-1; suppresses the phenotypic defects
FT of an RNA polymerase II CTD truncation."
FT /evidence="ECO:0000269|PubMed:8324825"
FT HELIX 4..25
FT /evidence="ECO:0007829|PDB:3R84"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:3R84"
FT HELIX 50..86
FT /evidence="ECO:0007829|PDB:3R84"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:4H62"
SQ SEQUENCE 121 AA; 13863 MW; 7703E4FAE101A31F CRC64;
MSNQALYEKL EQTRTILSVK LAELINMTTI ADRNDDDEGS FAQENSELAV ATTSVMMVNN
QTMQLIKNVQ DLLILTRSIK EKWLLNQIPV TEHSKVTRFD EKQIEELLDN CIETFVAEKT
T
