BOL1_YEAST
ID BOL1_YEAST Reviewed; 110 AA.
AC Q3E793; D6VPH1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=BolA-like protein 1 {ECO:0000305};
GN Name=BOL1 {ECO:0000303|PubMed:27532772, ECO:0000303|PubMed:27532773};
GN OrderedLocusNames=YAL044W-A;
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=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH
RP GRX5, AND MUTAGENESIS OF HIS-56 AND HIS-93.
RX PubMed=27532773; DOI=10.7554/elife.15991;
RA Melber A., Na U., Vashisht A., Weiler B.D., Lill R., Wohlschlegel J.A.,
RA Winge D.R.;
RT "Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial
RT clients.";
RL Elife 5:0-0(2016).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27532772; DOI=10.7554/elife.16673;
RA Uzarska M.A., Nasta V., Weiler B.D., Spantgar F., Ciofi-Baffoni S.,
RA Saviello M.R., Gonnelli L., Muehlenhoff U., Banci L., Lill R.;
RT "Mitochondrial Bol1 and Bol3 function as assembly factors for specific
RT iron-sulfur proteins.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly
CC factor that facilitates [4Fe-4S] cluster insertion into a subset of
CC mitochondrial proteins such as lipoyl synthase (LS) and succinate
CC dehydrogenase (SDH) (PubMed:27532772). Required during the last step of
CC iron-sulfur protein assembly when the iron-sulfur cluster is inserted
CC into the target protein (PubMed:27532772). Probably acts together with
CC the monothiol glutaredoxin GRX5, earlier than BOL3 and NFU1 in the
CC [4Fe-4S] cluster insertion process (PubMed:27532773). Not required for
CC [2Fe-2S] cluster insertion into mitochondrial proteins
CC (PubMed:27532772). {ECO:0000269|PubMed:27532772,
CC ECO:0000269|PubMed:27532773}.
CC -!- SUBUNIT: Interacts with GRX5. {ECO:0000269|PubMed:27532773}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:27532772, ECO:0000305|PubMed:27532773}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:27532773,
CC PubMed:27532772). Cells lacking BOL1 and BOL3 display defects in a
CC subset of mitochondrial [4Fe-4S] enzymes (PubMed:27532772).
CC {ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27532773}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BolA/IbaG family. {ECO:0000305}.
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DR EMBL; U12980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006935; DAA06941.1; -; Genomic_DNA.
DR RefSeq; NP_075206.1; NM_001184453.1.
DR AlphaFoldDB; Q3E793; -.
DR SMR; Q3E793; -.
DR BioGRID; 31782; 29.
DR ComplexPortal; CPX-6928; BOL1-GRX5 iron-sulfur cluster assembly complex.
DR IntAct; Q3E793; 4.
DR STRING; 4932.YAL044W-A; -.
DR MaxQB; Q3E793; -.
DR PaxDb; Q3E793; -.
DR PRIDE; Q3E793; -.
DR EnsemblFungi; YAL044W-A_mRNA; YAL044W-A; YAL044W-A.
DR GeneID; 851252; -.
DR KEGG; sce:YAL044W-A; -.
DR SGD; S000007586; BOL1.
DR VEuPathDB; FungiDB:YAL044W-A; -.
DR eggNOG; KOG2313; Eukaryota.
DR GeneTree; ENSGT00960000189278; -.
DR HOGENOM; CLU_109462_2_0_1; -.
DR InParanoid; Q3E793; -.
DR OMA; FNDSYKH; -.
DR BioCyc; YEAST:G3O-28901-MON; -.
DR PRO; PR:Q3E793; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; Q3E793; protein.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IC:ComplexPortal.
DR GO; GO:0044572; P:[4Fe-4S] cluster assembly; IMP:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IGI:SGD.
DR Gene3D; 3.30.300.90; -; 1.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR Pfam; PF01722; BolA; 1.
DR PIRSF; PIRSF003113; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome.
FT CHAIN 1..110
FT /note="BolA-like protein 1"
FT /id="PRO_0000248409"
FT MUTAGEN 56
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:27532773"
FT MUTAGEN 56
FT /note="H->C: Partial loss of function."
FT /evidence="ECO:0000269|PubMed:27532773"
FT MUTAGEN 93
FT /note="H->A,C: Loss of function."
FT /evidence="ECO:0000269|PubMed:27532773"
SQ SEQUENCE 110 AA; 12537 MW; BF19118A3F4FDA35 CRC64;
MFKRAMSTDG PVARTILKRL ECGFPDYKNF AFGLYNDSHK HKGHAGVQGN VSAETHFRIE
MVSKKFEGLK LPQRHRMVYS LLQDEMAQAN GIHALQLSLK TPQEYESKAK
