LSO2_YEAST
ID LSO2_YEAST Reviewed; 92 AA.
AC Q3E772; D6VUV3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein LSO2 {ECO:0000305};
DE AltName: Full=Late-annotated small open reading frame 2 {ECO:0000303|PubMed:26450372};
GN Name=LSO2 {ECO:0000303|PubMed:26450372};
GN OrderedLocusNames=YGR169C-A {ECO:0000312|SGD:S000028521};
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 GENOME REANNOTATION.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26450372; DOI=10.1002/mbo3.303;
RA An X., Zhang C., Sclafani R.A., Seligman P., Huang M.;
RT "The late-annotated small ORF LSO1 is a target gene of the iron regulon of
RT Saccharomyces cerevisiae.";
RL MicrobiologyOpen 4:941-951(2015).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30208026; DOI=10.1371/journal.pbio.2005903;
RA Wang Y.J., Vaidyanathan P.P., Rojas-Duran M.F., Udeshi N.D., Bartoli K.M.,
RA Carr S.A., Gilbert W.V.;
RT "Lso2 is a conserved ribosome-bound protein required for translational
RT recovery in yeast.";
RL PLoS Biol. 16:e2005903-e2005903(2018).
RN [7] {ECO:0007744|PDB:6Z6J, ECO:0007744|PDB:6Z6K}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), AND SUBUNIT.
RX PubMed=32687489; DOI=10.1371/journal.pbio.3000780;
RA Wells J.N., Buschauer R., Mackens-Kiani T., Best K., Kratzat H.,
RA Berninghausen O., Becker T., Gilbert W., Cheng J., Beckmann R.;
RT "Structure and function of yeast Lso2 and human CCDC124 bound to
RT hibernating ribosomes.";
RL PLoS Biol. 18:e3000780-e3000780(2020).
CC -!- FUNCTION: Ribosome-associated protein required for translational
CC recovery after starvation from stationary phase. May facilitate rapid
CC translation reactivation by stabilizing the recycling-competent state
CC of inactive ribosomes. {ECO:0000269|PubMed:30208026}.
CC -!- SUBUNIT: Associates with translationally inactive ribosomes in the
CC nonrotated state. LSO2 bridges the decoding sites of the small with the
CC GTPase activating center (GAC) of the large subunit. This position
CC allows accommodation of the DOM34-dependent ribosome recycling system,
CC which splits LSO2-containing ribosomes. {ECO:0000269|PubMed:32687489}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26450372}. Cytoplasm
CC {ECO:0000269|PubMed:26450372}. Note=Under iron-replete conditions,
CC enriched in the nucleus. Under iron-depleted conditions, expressed in
CC both nucleus and cytoplasm. {ECO:0000269|PubMed:26450372}.
CC -!- INDUCTION: Constitutively expressed. Expression is not regulated by
CC iron unlike the LSO1 paralog. {ECO:0000269|PubMed:26450372}.
CC -!- DISRUPTION PHENOTYPE: Mild slow-growth phenotype in response to reduced
CC iron levels (PubMed:26450372). Displays global translation defects
CC during recovery from stationary phase with translation of most genes
CC reduced more than 4-fold. Ribosomes accumulated at start codons, were
CC depleted from stop codons, and showed codon-specific changes in
CC occupancy (PubMed:30208026). {ECO:0000269|PubMed:26450372,
CC ECO:0000269|PubMed:30208026}.
CC -!- SIMILARITY: Belongs to the CCDC124 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z72954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006941; DAA08264.1; -; Genomic_DNA.
DR RefSeq; NP_878080.3; NM_001184531.3.
DR PDB; 6Z6J; EM; 3.40 A; C5=1-92.
DR PDB; 6Z6K; EM; 3.40 A; C5=2-92.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR AlphaFoldDB; Q3E772; -.
DR SMR; Q3E772; -.
DR BioGRID; 37002; 51.
DR IntAct; Q3E772; 2.
DR MINT; Q3E772; -.
DR STRING; 4932.YGR169C-A; -.
DR MaxQB; Q3E772; -.
DR PaxDb; Q3E772; -.
DR PRIDE; Q3E772; -.
DR EnsemblFungi; YGR169C-A_mRNA; YGR169C-A; YGR169C-A.
DR GeneID; 1466460; -.
DR KEGG; sce:YGR169C-A; -.
DR SGD; S000028521; LSO2.
DR VEuPathDB; FungiDB:YGR169C-A; -.
DR eggNOG; KOG3223; Eukaryota.
DR GeneTree; ENSGT00940000176679; -.
DR HOGENOM; CLU_186256_0_0_1; -.
DR InParanoid; Q3E772; -.
DR OMA; KWDQGSR; -.
DR BioCyc; YEAST:G3O-31009-MON; -.
DR PRO; PR:Q3E772; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q3E772; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IMP:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..92
FT /note="Protein LSO2"
FT /id="PRO_0000245386"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..80
FT /evidence="ECO:0000255"
FT COMPBIAS 13..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 92 AA; 10495 MW; 0B00892B34858428 CRC64;
MGKRFSESAA KKAAGLARKR DQAHAKQRAQ MEQLEAEEAS KWEQGSRKEN AKKLEEEQKR
QEKARAKKER DALLTAEEEQ LGKGGKGKRK MK
