RM51_YEAST
ID RM51_YEAST Reviewed; 140 AA.
AC Q06090; D6W498;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=54S ribosomal protein L51, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL43 {ECO:0000303|PubMed:24675956};
GN Name=MRPL51; OrderedLocusNames=YPR100W; ORFNames=P8283.12;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL LARGE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12392552; DOI=10.1046/j.1432-1033.2002.03226.x;
RA Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.;
RT "Tag-mediated isolation of yeast mitochondrial ribosome and mass
RT spectrometric identification of its new components.";
RL Eur. J. Biochem. 269:5203-5214(2002).
RN [4]
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 [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=25609543; DOI=10.1038/ncomms7019;
RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT "Organization of the mitochondrial translation machinery studied in situ by
RT cryoelectron tomography.";
RL Nat. Commun. 6:6019-6019(2015).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=31374566; DOI=10.1093/femsyr/foz056;
RA Sahu P.K., Salim S., Pp M., Chauhan S., Tomar R.S.;
RT "Reverse genetic analysis of yeast YPR099C/MRPL51 reveals a critical role
RT of both overlapping ORFs in respiratory growth and MRPL51 in mitochondrial
RT DNA maintenance.";
RL FEMS Yeast Res. 19:0-0(2019).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND SUBUNIT.
RX PubMed=24675956; DOI=10.1126/science.1249410;
RA Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F.,
RA Murshudov G., Scheres S.H., Ramakrishnan V.;
RT "Structure of the yeast mitochondrial large ribosomal subunit.";
RL Science 343:1485-1489(2014).
CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC mitochondrial genome-encoded proteins, including at least some of the
CC essential transmembrane subunits of the mitochondrial respiratory
CC chain. The mitoribosomes are attached to the mitochondrial inner
CC membrane and translation products are cotranslationally integrated into
CC the membrane (Probable). Also has an extraribosomal function, being
CC essential for mitochondrial genome integrity. May interact with MHR1 to
CC take part in the mtDNA repair mechanism (PubMed:25609543).
CC {ECO:0000269|PubMed:25609543, ECO:0000305|PubMed:24675956,
CC ECO:0000305|PubMed:25609543}.
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
CC and a large (54S) subunit. The 37S small subunit contains a 15S
CC ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
CC subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
CC {ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:24675956}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:31374566}.
CC Note=Mitoribosomes are tethered to the mitochondrial inner membrane and
CC spatially aligned with the membrane insertion machinery through two
CC distinct membrane contact sites, formed by the 21S rRNA expansion
CC segment 96-ES1 and the inner membrane protein MBA1.
CC {ECO:0000269|PubMed:25609543}.
CC -!- DISRUPTION PHENOTYPE: Has a respiratory growth defect. Shows complete
CC loss of growth on nonfermentable carbon source and a gradual loss of
CC mtDNA with replicative cell growth and an increasing number of
CC generations. {ECO:0000269|PubMed:31374566}.
CC -!- MISCELLANEOUS: Present with 3400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL43 family. {ECO:0000305}.
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DR EMBL; U32445; AAB68070.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11514.1; -; Genomic_DNA.
DR PIR; S59765; S59765.
DR RefSeq; NP_015425.1; NM_001184197.1.
DR PDB; 3J6B; EM; 3.20 A; 4=1-140.
DR PDB; 5MRC; EM; 3.25 A; 4=2-139.
DR PDB; 5MRE; EM; 3.75 A; 4=2-139.
DR PDB; 5MRF; EM; 4.97 A; 4=2-139.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; Q06090; -.
DR SMR; Q06090; -.
DR BioGRID; 36266; 92.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-6814N; -.
DR IntAct; Q06090; 8.
DR STRING; 4932.YPR100W; -.
DR MaxQB; Q06090; -.
DR PaxDb; Q06090; -.
DR PRIDE; Q06090; -.
DR EnsemblFungi; YPR100W_mRNA; YPR100W; YPR100W.
DR GeneID; 856214; -.
DR KEGG; sce:YPR100W; -.
DR SGD; S000006304; MRPL51.
DR VEuPathDB; FungiDB:YPR100W; -.
DR eggNOG; KOG3445; Eukaryota.
DR GeneTree; ENSGT00390000015375; -.
DR HOGENOM; CLU_117700_1_1_1; -.
DR InParanoid; Q06090; -.
DR OMA; ISKWIDL; -.
DR BioCyc; YEAST:G3O-34240-MON; -.
DR PRO; PR:Q06090; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06090; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR InterPro; IPR039927; MRPL43/MRPL51.
DR InterPro; IPR007741; Ribosome/NADH_DH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR21396; PTHR21396; 1.
DR Pfam; PF05047; L51_S25_CI-B8; 1.
DR SMART; SM00916; L51_S25_CI-B8; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..140
FT /note="54S ribosomal protein L51, mitochondrial"
FT /id="PRO_0000030590"
SQ SEQUENCE 140 AA; 16124 MW; 261C646FFE6E9EF3 CRC64;
MVVKAIARNS IGRNGVGAFV FPCRKITLQF CNWGGSSEGM RKFLTSKRLD KWGQEFPWIQ
FEVMRKSGHP LLRAEYTNGR EKVICVRNLN IDNVENKLKL LKDSDGDILR RRTKNDNVES
LNSSVRGIWS PLHAAKRHRI
