MHR1_YEAST
ID MHR1_YEAST Reviewed; 226 AA.
AC Q06630; D6VSS5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mitochondrial homologous recombination protein 1;
DE AltName: Full=Cross-linked transcription component 1;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL67 {ECO:0000303|PubMed:24675956};
GN Name=MHR1; Synonyms=XTC1; OrderedLocusNames=YDR296W;
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 FUNCTION.
RX PubMed=11121487; DOI=10.1093/nar/28.24.4956;
RA Ling F., Morioka H., Ohtsuka E., Shibata T.;
RT "A role for MHR1, a gene required for mitochondrial genetic recombination,
RT in the repair of damage spontaneously introduced in yeast mtDNA.";
RL Nucleic Acids Res. 28:4956-4963(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [5]
RP PROTEIN SEQUENCE OF 192-208, AND FUNCTION.
RX PubMed=9736700; DOI=10.1073/pnas.95.19.11122;
RA Emili A., Kobayashi R., Ingles C.J.;
RT "A novel yeast protein influencing the response of RNA polymerase II to
RT transcriptional activators.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11122-11127(1998).
RN [6]
RP FUNCTION.
RX PubMed=7664749; DOI=10.1002/j.1460-2075.1995.tb00081.x;
RA Ling F., Makishima F., Morishima N., Shibata T.;
RT "A nuclear mutation defective in mitochondrial recombination in yeast.";
RL EMBO J. 14:4090-4101(1995).
RN [7]
RP FUNCTION, MUTAGENESIS OF GLY-172, AND SUBCELLULAR LOCATION.
RX PubMed=12198175; DOI=10.1093/emboj/cdf466;
RA Ling F., Shibata T.;
RT "Recombination-dependent mtDNA partitioning: in vivo role of Mhr1p to
RT promote pairing of homologous DNA.";
RL EMBO J. 21:4730-4740(2002).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12034822; DOI=10.1093/nar/30.11.2358;
RA Traven A., Staresincic L., Arneric M., Sopta M.;
RT "The yeast protein Xtc1 functions as a direct transcriptional repressor.";
RL Nucleic Acids Res. 30:2358-2364(2002).
RN [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, AND MUTAGENESIS OF GLY-172.
RX PubMed=14565971; DOI=10.1091/mbc.e03-07-0508;
RA Ling F., Shibata T.;
RT "Mhr1p-dependent concatemeric mitochondrial DNA formation for generating
RT yeast mitochondrial homoplasmic cells.";
RL Mol. Biol. Cell 15:310-322(2004).
RN [13]
RP FUNCTION.
RX PubMed=16337661; DOI=10.1016/j.mrfmmm.2005.10.006;
RA Mookerjee S.A., Sia E.A.;
RT "Overlapping contributions of Msh1p and putative recombination proteins
RT Cce1p, Din7p, and Mhr1p in large-scale recombination and genome sorting
RT events in the mitochondrial genome of Saccharomyces cerevisiae.";
RL Mutat. Res. 595:91-106(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
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 [16]
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). mL67/MHR1 also has
CC extraribosomal functions, being involved in regulation of mitochondrial
CC DNA recombination, maintenance and repair, and generation of
CC homoplasmic cells (PubMed:11121487, PubMed:12198175, PubMed:14565971,
CC PubMed:16337661, PubMed:7664749, PubMed:9736700). mL67/MHR1 also acts
CC as transcription factor involved in regulation of RNA polymerase II-
CC dependent transcription (PubMed:12034822).
CC {ECO:0000269|PubMed:11121487, ECO:0000269|PubMed:12034822,
CC ECO:0000269|PubMed:12198175, ECO:0000269|PubMed:14565971,
CC ECO:0000269|PubMed:16337661, ECO:0000269|PubMed:7664749,
CC ECO:0000269|PubMed:9736700, 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:24675956}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12034822}.
CC Mitochondrion {ECO:0000269|PubMed:12034822,
CC ECO:0000269|PubMed:12198175, 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 -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL67 family. {ECO:0000305}.
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DR EMBL; AB016430; BAA88081.1; -; Genomic_DNA.
DR EMBL; U28374; AAB64732.1; -; Genomic_DNA.
DR EMBL; AY557735; AAS56061.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12135.1; -; Genomic_DNA.
DR PIR; S61182; S61182.
DR RefSeq; NP_010582.3; NM_001180604.3.
DR PDB; 3J6B; EM; 3.20 A; d=1-226.
DR PDB; 5MRC; EM; 3.25 A; d=1-215.
DR PDB; 5MRE; EM; 3.75 A; d=1-215.
DR PDB; 5MRF; EM; 4.97 A; d=1-215.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; Q06630; -.
DR BMRB; Q06630; -.
DR SMR; Q06630; -.
DR BioGRID; 32348; 103.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-5727N; -.
DR IntAct; Q06630; 48.
DR MINT; Q06630; -.
DR STRING; 4932.YDR296W; -.
DR iPTMnet; Q06630; -.
DR MaxQB; Q06630; -.
DR PaxDb; Q06630; -.
DR PRIDE; Q06630; -.
DR EnsemblFungi; YDR296W_mRNA; YDR296W; YDR296W.
DR GeneID; 851890; -.
DR KEGG; sce:YDR296W; -.
DR SGD; S000002704; MHR1.
DR VEuPathDB; FungiDB:YDR296W; -.
DR eggNOG; ENOG502QSKX; Eukaryota.
DR HOGENOM; CLU_092898_0_0_1; -.
DR InParanoid; Q06630; -.
DR OMA; WENRKPS; -.
DR BioCyc; YEAST:G3O-29858-MON; -.
DR PRO; PR:Q06630; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06630; 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:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IPI:SGD.
DR InterPro; IPR024629; Mhr1.
DR PANTHER; PTHR28184; PTHR28184; 1.
DR Pfam; PF12829; Mhr1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transcription;
KW Transcription regulation.
FT CHAIN 1..226
FT /note="Mitochondrial homologous recombination protein 1"
FT /id="PRO_0000255967"
FT MUTAGEN 172
FT /note="G->D: In MHR1-1; causes a defect in the partitioning
FT of nascent mtDNA into buds and delays generation of
FT homoplasmic cells."
FT /evidence="ECO:0000269|PubMed:12198175,
FT ECO:0000269|PubMed:14565971"
SQ SEQUENCE 226 AA; 26895 MW; F26903A4814091C4 CRC64;
MKVNHSISRF RPASWFEKTK IIPPQVYIFR NLEYGQVLYS QFPNFSQTQV DKLFVRPNWS
NRKPSLRRDI WKCMCVVNLQ NYKQSVHLYQ NLCRLRYLRD VAQRKESDKL RKKDSNGHVW
YSGQYRPTYC QEAVADLRES LLKVFENATP AEKQTVPAKK PSIYWEDPWR MGDKDKHWNY
DVFNALGLEH KLIQRVGNIA REESVILKEL AKLESHPTEQ TEVSSQ
