RM36_YEAST
ID RM36_YEAST Reviewed; 177 AA.
AC P36531; D6VQC0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=54S ribosomal protein L36, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL31m {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL36;
DE Flags: Precursor;
GN Name=MRPL36; OrderedLocusNames=YBR122C; ORFNames=YBR0918;
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 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
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 [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 PROTEIN SEQUENCE OF 15-51, AND SUBUNIT.
RC STRAIN=07173;
RX PubMed=2060626; DOI=10.1016/0014-5793(91)80759-v;
RA Grohmann L., Graack H.-R., Kruft V., Choli T., Goldschmidt-Reisin S.,
RA Kitakawa M.;
RT "Extended N-terminal sequencing of proteins of the large ribosomal subunit
RT from yeast mitochondria.";
RL FEBS Lett. 284:51-56(1991).
RN [5]
RP FUNCTION.
RX PubMed=11259585; DOI=10.1128/mcb.21.7.2359-2372.2001;
RA Bonnefoy N., Bsat N., Fox T.D.;
RT "Mitochondrial translation of Saccharomyces cerevisiae COX2 mRNA is
RT controlled by the nucleotide sequence specifying the pre-Cox2p leader
RT peptide.";
RL Mol. Cell. Biol. 21:2359-2372(2001).
RN [6]
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 [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
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 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 [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=15166137; DOI=10.1534/genetics.167.1.65;
RA Williams E.H., Perez-Martinez X., Fox T.D.;
RT "MrpL36p, a highly diverged L31 ribosomal protein homolog with additional
RT functional domains in Saccharomyces cerevisiae mitochondria.";
RL Genetics 167:65-75(2004).
RN [11]
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 [12]
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 (PubMed:25609543, PubMed:24675956). Overexpression of
CC bL31m suppresses mutations in the COX2 leader peptide-encoding and
CC initiation codon regions (PubMed:11259585, PubMed:15166137).
CC {ECO:0000269|PubMed:11259585, ECO:0000269|PubMed:15166137,
CC ECO:0000305|PubMed:24675956, ECO:0000305|PubMed:25609543}.
CC -!- FUNCTION: Overexpression suppresses mutations in the COX2 leader
CC peptide-encoding and initiation codon regions.
CC {ECO:0000269|PubMed:11259585, ECO:0000269|PubMed:15166137}.
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:2060626,
CC ECO:0000269|PubMed:24675956}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the
CC mitochondrial inner membrane and spatially aligned with the membrane
CC insertion machinery through two distinct membrane contact sites, formed
CC by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein
CC MBA1. {ECO:0000269|PubMed:25609543}.
CC -!- DOMAIN: Contains two functional domains. The central domain is
CC sufficient for general mitochondrial translation but not suppression of
CC COX2 mutants. The C-terminus sequence is sufficient for dosage
CC suppression of COX2 mutants. {ECO:0000269|PubMed:15166137}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family.
CC Highly divergent. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA85079.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X78993; CAA55624.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z35991; CAA85079.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07240.1; -; Genomic_DNA.
DR PIR; S44701; S44701.
DR RefSeq; NP_009680.2; NM_001178470.1.
DR PDB; 3J6B; EM; 3.20 A; V=1-177.
DR PDB; 5MRC; EM; 3.25 A; V=1-177.
DR PDB; 5MRE; EM; 3.75 A; V=1-177.
DR PDB; 5MRF; EM; 4.97 A; V=1-177.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P36531; -.
DR SMR; P36531; -.
DR BioGRID; 32824; 157.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-4628N; -.
DR IntAct; P36531; 15.
DR MINT; P36531; -.
DR STRING; 4932.YBR122C; -.
DR MaxQB; P36531; -.
DR PaxDb; P36531; -.
DR PRIDE; P36531; -.
DR EnsemblFungi; YBR122C_mRNA; YBR122C; YBR122C.
DR GeneID; 852419; -.
DR KEGG; sce:YBR122C; -.
DR SGD; S000000326; MRPL36.
DR VEuPathDB; FungiDB:YBR122C; -.
DR eggNOG; ENOG502RZ6E; Eukaryota.
DR HOGENOM; CLU_130029_1_0_1; -.
DR InParanoid; P36531; -.
DR OMA; RRSQFPK; -.
DR BioCyc; YEAST:G3O-29079-MON; -.
DR PRO; PR:P36531; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P36531; 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; HDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR InterPro; IPR034600; MRPL36_yeast.
DR PANTHER; PTHR28174; PTHR28174; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2060626"
FT CHAIN 15..177
FT /note="54S ribosomal protein L36, mitochondrial"
FT /id="PRO_0000030580"
FT REGION 36..118
FT /note="Sufficient for general mitochondrial translation"
FT REGION 87..177
FT /note="Sufficient for dosage suppression of COX2 mutation"
FT REGION 111..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 20091 MW; 7A8DF86EE899B848 CRC64;
MLKSIFAKRF ASTGSYPGST RITLPRRPAK KIQLGKSRPA IYHQFNVKME LSDGSVVIRR
SQYPKGEIRL IQDQRNNPLW NPSRDDLVVV DANSGGSLDR FNKRYSSLFS VDSTTPNSSS
ETVELSEENK KKTQIKKEEK EDVSEKAFGM DDYLSLLDDS EQQIKSGKLA SKKRDKK
