BOL3_YEAST
ID BOL3_YEAST Reviewed; 118 AA.
AC P39724; D6VPH0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=BolA-like protein 3 {ECO:0000305};
DE AltName: Full=Altered inheritance of mitochondria protein 1;
GN Name=BOL3 {ECO:0000303|PubMed:27532772, ECO:0000303|PubMed:27532773};
GN Synonyms=AIM1; OrderedLocusNames=YAL046C;
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 DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH
RP NFU1, AND MUTAGENESIS OF CYS-64 AND HIS-101.
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 [6]
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:27532773, PubMed:27532772). Required during
CC the last step of iron-sulfur protein assembly when the iron-sulfur
CC cluster is inserted into the target protein (PubMed:27532772). Acts
CC together with NFU1, later than BOL1 and GRX5 in the [4Fe-4S] cluster
CC insertion process (PubMed:27532773). Not required for [2Fe-2S] cluster
CC insertion into mitochondrial proteins (PubMed:27532772).
CC {ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27532773}.
CC -!- SUBUNIT: Interacts with NFU1 (PubMed:27532773).
CC {ECO:0000269|PubMed:27532773}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:27532772, ECO:0000305|PubMed:27532773}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss
CC (PubMed:19300474). Cells show a slight decrease of succinate
CC dehydrogenase (SDH) (PubMed:27532772). Cells lacking BOL1 and BOL3
CC display defects in a subset of mitochondrial [4Fe-4S] enzymes
CC (PubMed:27532773, PubMed:27532772). {ECO:0000269|PubMed:19300474,
CC ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27532773}.
CC -!- MISCELLANEOUS: Present with 259 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; AAC04985.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06940.1; -; Genomic_DNA.
DR PIR; S51973; S51973.
DR RefSeq; NP_009353.1; NM_001178191.1.
DR AlphaFoldDB; P39724; -.
DR SMR; P39724; -.
DR BioGRID; 31781; 111.
DR ComplexPortal; CPX-6930; BOL3-GRX5 iron-sulfur cluster assembly complex.
DR IntAct; P39724; 3.
DR MINT; P39724; -.
DR STRING; 4932.YAL046C; -.
DR MaxQB; P39724; -.
DR PaxDb; P39724; -.
DR PRIDE; P39724; -.
DR EnsemblFungi; YAL046C_mRNA; YAL046C; YAL046C.
DR GeneID; 851251; -.
DR KEGG; sce:YAL046C; -.
DR SGD; S000000044; BOL3.
DR VEuPathDB; FungiDB:YAL046C; -.
DR eggNOG; KOG3348; Eukaryota.
DR GeneTree; ENSGT00390000013048; -.
DR HOGENOM; CLU_109462_0_1_1; -.
DR InParanoid; P39724; -.
DR OMA; MFAISIE; -.
DR BioCyc; YEAST:G3O-28853-MON; -.
DR PRO; PR:P39724; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39724; protein.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IC:ComplexPortal.
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; IMP:SGD.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR Pfam; PF01722; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome.
FT CHAIN 1..118
FT /note="BolA-like protein 3"
FT /id="PRO_0000201239"
FT MUTAGEN 64
FT /note="C->A: Partial loss of function."
FT /evidence="ECO:0000269|PubMed:27532773"
FT MUTAGEN 101
FT /note="H->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:27532773"
FT MUTAGEN 101
FT /note="H->C: Dominant negative mutant; displays respiratory
FT defects that are higher than the BOL1 BOL3 double mutant."
FT /evidence="ECO:0000269|PubMed:27532773"
SQ SEQUENCE 118 AA; 13356 MW; 244F5FF2052FF410 CRC64;
MKLPQTMLRS ISVKHVRWPR ILTGSKLWYS TQMAMTPEEK MITDKLQQEL EPEVCKVQDV
SGGCGSMFAI NITSKKFNGL SLIKQHQLVN RILRDDISRW HGLQLTTKKS TGKGPASS
