MED11_YEAST
ID MED11_YEAST Reviewed; 115 AA.
AC Q99278; D6VZT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 11;
DE AltName: Full=Mediator complex subunit 11;
GN Name=MED11; OrderedLocusNames=YMR112C; ORFNames=YM9718.11C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=9812975; DOI=10.1074/jbc.273.47.30851;
RA Gustafsson C.M., Myers L.C., Beve J., Spaahr H., Lui M.,
RA Erdjument-Bromage H., Tempst P., Kornberg R.D.;
RT "Identification of new mediator subunits in the RNA polymerase II
RT holoenzyme from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:30851-30854(1998).
RN [5]
RP INTERACTION WITH SRB4.
RX PubMed=11555651; DOI=10.1074/jbc.m105961200;
RA Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.;
RT "The structural and functional organization of the yeast mediator
RT complex.";
RL J. Biol. Chem. 276:42003-42010(2001).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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).
RN [14]
RP IDENTIFICATION OF INITIATION SITE.
RX PubMed=17101987; DOI=10.1073/pnas.0605645103;
RA Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S.,
RA Ito T.;
RT "A large-scale full-length cDNA analysis to explore the budding yeast
RT transcriptome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006).
RN [15]
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 [16]
RP FUNCTION, INTERACTION WITH SRB4; SRB6 AND RAD3, AND MUTAGENESIS OF THR-31
RP AND GLY-92.
RX PubMed=18691966; DOI=10.1016/j.molcel.2008.06.021;
RA Esnault C., Ghavi-Helm Y., Brun S., Soutourina J., Van Berkum N.,
RA Boschiero C., Holstege F., Werner M.;
RT "Mediator-dependent recruitment of TFIIH modules in preinitiation
RT complex.";
RL Mol. Cell 31:337-346(2008).
RN [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (4.3 ANGSTROMS) OF 1-115.
RX PubMed=21725323; DOI=10.1038/nature10162;
RA Imasaki T., Calero G., Cai G., Tsai K.-L., Yamada K., Cardelli F.,
RA Erdjument-Bromage H., Tempst P., Berger I., Kornberg G.L., Asturias F.J.,
RA Kornberg R.D., Takagi Y.;
RT "Architecture of the Mediator head module.";
RL Nature 475:240-243(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 5-89 IN COMPLEX WITH SRB6,
RP INTERACTION WITH SRB4, IDENTIFICATION OF INITIATION SITE, AND MUTAGENESIS
RP OF GLU-17 AND LEU-24.
RX PubMed=21498544; DOI=10.1093/nar/gkr229;
RA Seizl M., Lariviere L., Pfaffeneder T., Wenzeck L., Cramer P.;
RT "Mediator head subcomplex Med11/22 contains a common helix bundle building
RT block with a specific function in transcription initiation complex
RT stabilization.";
RL Nucleic Acids Res. 39:6291-6304(2011).
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 (PIC) with RNA polymerase II and the
CC general transcription factors. The Mediator complex unfolds to an
CC extended conformation and partially surrounds RNA polymerase II,
CC specifically interacting with the unphosphorylated form of the C-
CC terminal domain (CTD) of RNA polymerase II. The Mediator complex
CC dissociates from the RNA polymerase II holoenzyme and stays at the
CC promoter when transcriptional elongation begins. The essential MED11/22
CC heterodimer specifically functions in promoting stable PIC formation.
CC {ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16263706,
CC ECO:0000269|PubMed:16885025, ECO:0000269|PubMed:18691966}.
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. MED11 forms a
CC heterodimer with SRB6/MED22. The MED11/22 heterodimer binds to and
CC stabilizes the central head subunit SRB4/MED17. Interacts with TFIIH
CC subunit RAD3. {ECO:0000269|PubMed:11555651,
CC ECO:0000269|PubMed:16885025, ECO:0000269|PubMed:17192271,
CC ECO:0000269|PubMed:18691966, ECO:0000269|PubMed:21498544}.
CC -!- INTERACTION:
CC Q99278; P32569: SRB4; NbExp=21; IntAct=EBI-27213, EBI-18025;
CC Q99278; P32570: SRB6; NbExp=17; IntAct=EBI-27213, EBI-18039;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mediator complex subunit 11 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56732.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA89748.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA89749.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA10009.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z49702; CAA89749.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49702; CAA89748.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY558406; AAS56732.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006946; DAA10009.1; ALT_INIT; Genomic_DNA.
DR PIR; S54573; S54573.
DR RefSeq; NP_013830.1; NM_001182612.1.
DR PDB; 3J1O; EM; 16.00 A; H=2-115.
DR PDB; 3R84; X-ray; 2.05 A; A/C/E/G/I/K/M/O/Q/S/U/W=5-89.
DR PDB; 3RJ1; X-ray; 4.30 A; A/H/O=2-115.
DR PDB; 4GWP; X-ray; 4.20 A; A=1-115.
DR PDB; 4GWQ; X-ray; 4.50 A; A=1-115.
DR PDB; 4H62; X-ray; 3.00 A; K=84-115.
DR PDB; 4V1O; EM; 9.70 A; V=1-115.
DR PDB; 5OQM; EM; 5.80 A; c=1-115.
DR PDB; 5SVA; EM; 15.30 A; O=1-115.
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; Q99278; -.
DR SMR; Q99278; -.
DR BioGRID; 35288; 466.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-1434N; -.
DR IntAct; Q99278; 34.
DR MINT; Q99278; -.
DR STRING; 4932.YMR112C; -.
DR MaxQB; Q99278; -.
DR PaxDb; Q99278; -.
DR PeptideAtlas; Q99278; -.
DR PRIDE; Q99278; -.
DR GeneID; 855139; -.
DR KEGG; sce:YMR112C; -.
DR SGD; S000004718; MED11.
DR eggNOG; ENOG502S3YW; Eukaryota.
DR HOGENOM; CLU_121031_1_0_1; -.
DR InParanoid; Q99278; -.
DR BioCyc; YEAST:G3O-32808-MON; -.
DR PRO; PR:Q99278; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q99278; 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:0001097; F:TFIIH-class transcription factor complex binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP: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; IPR019404; Mediator_Med11.
DR Pfam; PF10280; Med11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..115
FT /note="Mediator of RNA polymerase II transcription subunit
FT 11"
FT /id="PRO_0000096358"
FT COILED 56..107
FT /evidence="ECO:0000255"
FT MUTAGEN 17
FT /note="E->K: Results in a decrease of TFIIK and RNA
FT polymerase II occupancies at active promoters; when
FT associated with K-24."
FT /evidence="ECO:0000269|PubMed:21498544"
FT MUTAGEN 24
FT /note="L->K: Results in a decrease of TFIIK and RNA
FT polymerase II occupancies at active promoters; when
FT associated with K-17."
FT /evidence="ECO:0000269|PubMed:21498544"
FT MUTAGEN 31
FT /note="T->A: Impairs interaction with RAD3, reducing the
FT interaction of TFIIH with the head module and consequently
FT resulting in a reduction of RNA polymerase II CTD 'Ser-5'
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:18691966"
FT MUTAGEN 66
FT /note="L->P: Impairs interaction with SRB4/MED17,
FT SRB6/MED22 and RAD3."
FT MUTAGEN 92
FT /note="G->S: Impairs interaction with SRB4/MED17."
FT /evidence="ECO:0000269|PubMed:18691966"
FT HELIX 5..38
FT /evidence="ECO:0007829|PDB:3R84"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3R84"
FT HELIX 45..75
FT /evidence="ECO:0007829|PDB:3R84"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3R84"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:4H62"
SQ SEQUENCE 115 AA; 13307 MW; 457D13C6030F33CC CRC64;
MQPPYIQERL KSLNDIETQL CSMLQEASQV TFIFGELKRG NESVKPQFEN HVKQFYERLD
KSTTQLRKEI QLLDENVGTR LLPINVNKKA LGQDTEKMEE QLDLLSAILD PSKSK
