MSS51_YEAST
ID MSS51_YEAST Reviewed; 436 AA.
AC P32335; D6VYK4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein MSS51, mitochondrial;
DE AltName: Full=Mitochondrial splicing suppressor protein 51;
DE Flags: Precursor;
GN Name=MSS51; OrderedLocusNames=YLR203C; ORFNames=L8167.17;
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 204510 / AB320;
RX PubMed=6297789; DOI=10.1016/0092-8674(83)90498-1;
RA Faye G., Simon M.;
RT "Analysis of a yeast nuclear gene involved in the maturation of
RT mitochondrial pre-messenger RNA of the cytochrome oxidase subunit I.";
RL Cell 32:77-87(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D273-10B/A;
RX PubMed=1523888; DOI=10.1002/yea.320080707;
RA Simon M., della Seta F., Sor F., Faye G.;
RT "Analysis of the MSS51 region on chromosome XII of Saccharomyces
RT cerevisiae.";
RL Yeast 8:559-567(1992).
RN [3]
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 [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 FUNCTION.
RX PubMed=6320175; DOI=10.1073/pnas.81.1.8;
RA Simon M., Faye G.;
RT "Steps in processing of the mitochondrial cytochrome oxidase subunit I pre-
RT mRNA affected by a nuclear mutation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:8-12(1984).
RN [6]
RP CHARACTERIZATION.
RX PubMed=2177521; DOI=10.1007/bf00259457;
RA Decoster E., Simon M., Hatat D., Faye G.;
RT "The MSS51 gene product is required for the translation of the COX1 mRNA in
RT yeast mitochondria.";
RL Mol. Gen. Genet. 224:111-118(1990).
RN [7]
RP FUNCTION IN TRANSLATION REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=10803883; DOI=10.1007/s002940050522;
RA Siep M., van Oosterum K., Neufeglise H., van der Spek H., Grivell L.A.;
RT "Mss51p, a putative translational activator of cytochrome c oxidase
RT subunit-1 (COX1) mRNA, is required for synthesis of Cox1p in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 37:213-220(2000).
RN [8]
RP MUTAGENESIS OF THR-167 AND PHE-199.
RX PubMed=11782424; DOI=10.1093/emboj/21.1.43;
RA Barrientos A., Korr D., Tzagoloff A.;
RT "Shy1p is necessary for full expression of mitochondrial COX1 in the yeast
RT model of Leigh's syndrome.";
RL EMBO J. 21:43-52(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH COX1.
RX PubMed=14592991; DOI=10.1093/emboj/cdg566;
RA Perez-Martinez X., Broadley S.A., Fox T.D.;
RT "Mss51p promotes mitochondrial Cox1p synthesis and interacts with newly
RT synthesized Cox1p.";
RL EMBO J. 22:5951-5961(2003).
RN [10]
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 [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).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH COX1 AND COX14.
RX PubMed=15306853; DOI=10.1038/sj.emboj.7600358;
RA Barrientos A., Zambrano A., Tzagoloff A.;
RT "Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in
RT Saccharomyces cerevisiae.";
RL EMBO J. 23:3472-3482(2004).
CC -!- FUNCTION: Has a dual role in the assembly of cytochrome oxidase subunit
CC 1 (COX1). It has a regulative function on COX1 synthesis, acting as a
CC translational activator specific for the COX1 mRNA, and it also binds
CC to newly synthesized COX1 protein. Together with COX14, may act as a
CC chaperone that binds efficiently unassembled COX1 and prevents it from
CC unproductive aggregation. When bound to COX1, MSS51 is unable to
CC interact with the COX1 mRNA and translation is halted. This may be a
CC feedback control that ensures that COX1 is only produced as long as
CC potentially harmful assembly intermediates are not accumulating.
CC {ECO:0000269|PubMed:10803883, ECO:0000269|PubMed:14592991,
CC ECO:0000269|PubMed:15306853, ECO:0000269|PubMed:6320175}.
CC -!- SUBUNIT: Interacts with COX1 and COX14. {ECO:0000269|PubMed:14592991,
CC ECO:0000269|PubMed:15306853}.
CC -!- INTERACTION:
CC P32335; P40452: COA1; NbExp=3; IntAct=EBI-11318, EBI-25287;
CC P32335; Q3E7B2: COA3; NbExp=4; IntAct=EBI-11318, EBI-3680840;
CC P32335; P39103: COX14; NbExp=3; IntAct=EBI-11318, EBI-5113;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10803883, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15306853}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10803883,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:15306853}; Matrix side {ECO:0000269|PubMed:10803883,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:15306853}.
CC -!- MISCELLANEOUS: Present with 4800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MSS51 family. {ECO:0000305}.
CC -!- CAUTION: Although no clear MSS51 ortholog is encoded in mammalian
CC genomes, the mammalian MSS51/ZMYND17 protein of unknown function is
CC significantly similar. {ECO:0000305}.
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DR EMBL; J01487; AAA66926.1; -; Genomic_DNA.
DR EMBL; S43721; AAB23218.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67438.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09520.1; -; Genomic_DNA.
DR PIR; S48554; S42160.
DR RefSeq; NP_013304.1; NM_001182090.1.
DR AlphaFoldDB; P32335; -.
DR BioGRID; 31471; 145.
DR ComplexPortal; CPX-1423; COX1 pre-assembly complex.
DR DIP; DIP-4602N; -.
DR IntAct; P32335; 9.
DR MINT; P32335; -.
DR STRING; 4932.YLR203C; -.
DR iPTMnet; P32335; -.
DR MaxQB; P32335; -.
DR PaxDb; P32335; -.
DR PRIDE; P32335; -.
DR DNASU; 850900; -.
DR EnsemblFungi; YLR203C_mRNA; YLR203C; YLR203C.
DR GeneID; 850900; -.
DR KEGG; sce:YLR203C; -.
DR SGD; S000004193; MSS51.
DR VEuPathDB; FungiDB:YLR203C; -.
DR eggNOG; ENOG502QQBW; Eukaryota.
DR HOGENOM; CLU_033072_0_0_1; -.
DR InParanoid; P32335; -.
DR OMA; NWGLWAF; -.
DR BioCyc; YEAST:G3O-32322-MON; -.
DR PRO; PR:P32335; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32335; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0045182; F:translation regulator activity; IMP:SGD.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070130; P:negative regulation of mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR032717; Mss51_Znf.
DR InterPro; IPR013272; Vps72/YL1_C.
DR Pfam; PF13824; zf-Mss51; 1.
DR SMART; SM00993; YL1_C; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW mRNA splicing; Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..436
FT /note="Protein MSS51, mitochondrial"
FT /id="PRO_0000096603"
FT REGION 43..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 167
FT /note="T->R: Partially suppresses the respiratory defect of
FT SHY1 mutants by increasing COX1 translation."
FT /evidence="ECO:0000269|PubMed:11782424"
FT MUTAGEN 199
FT /note="F->I: Partially suppresses the respiratory defect of
FT SHY1 mutants by increasing COX1 translation."
FT /evidence="ECO:0000269|PubMed:11782424"
FT CONFLICT 210
FT /note="I -> M (in Ref. 1; AAA66926 and 2; AAB23218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 50880 MW; 6A55BF160FE1D7DE CRC64;
MTVLYAPSGA TQLYFHLLRK SPHNRLVVSH QTRRHLMGFV RNALGLDPPP SPEDPTPENR
FHPWDQSPSV DLRERAAKIR TLAHCPVTGK DINYTCPLSG IPTHHSREAW EMDKAYHDSK
KYEILKKVNI YEHDLRSGRP FPEFDFPQQQ GYDKAVNLTN WDLFFYTRSF YSMDTEFQLA
AVTKMLSYPI TIGSLLHKFS PYSLNPKGPI TLEGLKSLAA LRYTLYPLEN RSLPTTTKNR
AMRIFILGAR AEAQLPGHVW KQLQFLFPEQ SFEIHFIGPE CLYKRDKQEY VKSTTPVVQR
VDETLKFIYR TNFFEVFHEA QDFFPYDPYM DVFFTFHPGY ASPESHGSWM GETMKALLET
KCAIFTTGFN KKDLTDDINL VKSKYGKEMD VLMEPVRNVF GSTKWELNDM NPQEVYQFNM
YIAGFRGKRY HTIKRQ
