ISU1_YEAST
ID ISU1_YEAST Reviewed; 165 AA.
AC Q03020; D6W3N2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Iron sulfur cluster assembly protein 1, mitochondrial;
DE AltName: Full=Iron sulfur cluster scaffold protein 1;
DE Flags: Precursor;
GN Name=ISU1; Synonyms=NUA1; OrderedLocusNames=YPL135W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION, PATHWAY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-69; CYS-96 AND CYS-139.
RX PubMed=10588895; DOI=10.1006/jmbi.1999.3294;
RA Garland S.A., Hoff K., Vickery L.E., Culotta V.C.;
RT "Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene
RT family for iron-sulfur cluster assembly.";
RL J. Mol. Biol. 294:897-907(1999).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10468587; DOI=10.1073/pnas.96.18.10206;
RA Schilke B., Voisine C., Beinert H., Craig E.;
RT "Evidence for a conserved system for iron metabolism in the mitochondria of
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10206-10211(1999).
RN [5]
RP FUNCTION, AND COFACTOR.
RX PubMed=12970193; DOI=10.1093/emboj/cdg446;
RA Muehlenhoff U., Gerber J., Richhardt N., Lill R.;
RT "Components involved in assembly and dislocation of iron-sulfur clusters on
RT the scaffold protein Isu1p.";
RL EMBO J. 22:4815-4825(2003).
RN [6]
RP INTERACTION WITH FRATAXIN.
RX PubMed=12947415; DOI=10.1038/sj.embor.embor918;
RA Gerber J., Muhlenhoff U., Lill R.;
RT "An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S
RT cluster synthesis on Isu1.";
RL EMBO Rep. 4:906-911(2003).
RN [7]
RP INTERACTION WITH JAC1 AND SSQ1.
RX PubMed=12756240; DOI=10.1074/jbc.m303527200;
RA Dutkiewicz R., Schilke B., Knieszner H., Walter W., Craig E.A.,
RA Marszalek J.;
RT "Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center
RT biogenesis. Similarities to and differences from its bacterial
RT counterpart.";
RL J. Biol. Chem. 278:29719-29727(2003).
RN [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH FRATAXIN.
RX PubMed=14741370; DOI=10.1016/s0014-5793(03)01498-4;
RA Ramazzotti A., Vanmansart V., Foury F.;
RT "Mitochondrial functional interactions between frataxin and Isu1p, the
RT iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae.";
RL FEBS Lett. 557:215-220(2004).
RN [10]
RP FUNCTION, INTERACTION WITH JAC1 AND SSQ1, AND MUTAGENESIS OF LEU-132;
RP PRO-133; PRO-134; VAL-135 AND LYS-136.
RX PubMed=15123690; DOI=10.1074/jbc.m402947200;
RA Dutkiewicz R., Schilke B., Cheng S., Knieszner H., Craig E.A.,
RA Marszalek J.;
RT "Sequence-specific interaction between mitochondrial Fe-S scaffold protein
RT Isu and Hsp70 Ssq1 is essential for their in vivo function.";
RL J. Biol. Chem. 279:29167-29174(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15143178; DOI=10.1128/mcb.24.11.4848-4857.2004;
RA Gerber J., Neumann K., Prohl C., Muehlenhoff U., Lill R.;
RT "The yeast scaffold proteins Isu1p and Isu2p are required inside
RT mitochondria for maturation of cytosolic Fe/S proteins.";
RL Mol. Cell. Biol. 24:4848-4857(2004).
RN [12]
RP FUNCTION.
RX PubMed=16341089; DOI=10.1038/sj.emboj.7600906;
RA Wiedemann N., Urzica E., Guiard B., Mueller H., Lohaus C., Meyer H.E.,
RA Ryan M.T., Meisinger C., Muehlenhoff U., Lill R., Pfanner N.;
RT "Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on
RT Isu scaffold proteins.";
RL EMBO J. 25:184-195(2006).
RN [13]
RP FUNCTION.
RX PubMed=16431909; DOI=10.1074/jbc.m513301200;
RA Dutkiewicz R., Marszalek J., Schilke B., Craig E.A., Lill R.,
RA Muehlenhoff U.;
RT "The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation
RT on the scaffold protein Isu1p.";
RL J. Biol. Chem. 281:7801-7808(2006).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [15]
RP INTERACTION WITH FRATAXIN.
RX PubMed=20815377; DOI=10.1021/bi1008613;
RA Cook J.D., Kondapalli K.C., Rawat S., Childs W.C., Murugesan Y., Dancis A.,
RA Stemmler T.L.;
RT "Molecular details of the yeast frataxin-Isu1 interaction during
RT mitochondrial Fe-S cluster assembly.";
RL Biochemistry 49:8756-8765(2010).
RN [16]
RP INTERACTION WITH JAC1.
RX PubMed=22306468; DOI=10.1016/j.jmb.2012.01.022;
RA Ciesielski S.J., Schilke B.A., Osipiuk J., Bigelow L., Mulligan R.,
RA Majewska J., Joachimiak A., Marszalek J., Craig E.A., Dutkiewicz R.;
RT "Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is
RT indispensable in vivo and conserved in evolution.";
RL J. Mol. Biol. 417:1-12(2012).
RN [17]
RP INTERACTION WITH JAC1 AND NFS1, AND MUTAGENESIS OF LEU-63; VAL-72 AND
RP PHE-94.
RX PubMed=23946486; DOI=10.1074/jbc.m113.503524;
RA Majewska J., Ciesielski S.J., Schilke B., Kominek J., Blenska A.,
RA Delewski W., Song J.Y., Marszalek J., Craig E.A., Dutkiewicz R.;
RT "Binding of the chaperone Jac1 protein and cysteine desulfurase Nfs1 to the
RT iron-sulfur cluster scaffold Isu protein is mutually exclusive.";
RL J. Biol. Chem. 288:29134-29142(2013).
RN [18]
RP FUNCTION, COFACTOR, INTERACTION WITH JAC1 AND SSQ1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23615440; DOI=10.1091/mbc.e12-09-0644;
RA Uzarska M.A., Dutkiewicz R., Freibert S.A., Lill R., Muehlenhoff U.;
RT "The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer
RT from Isu1 to Grx5 by complex formation.";
RL Mol. Biol. Cell 24:1830-1841(2013).
RN [19]
RP INTERACTION WITH FRATAXIN AND NFS1, AND MUTAGENESIS OF 134-PRO--LYS-136.
RX PubMed=25228696; DOI=10.1074/jbc.m114.596726;
RA Manicki M., Majewska J., Ciesielski S., Schilke B., Blenska A., Kominek J.,
RA Marszalek J., Craig E.A., Dutkiewicz R.;
RT "Overlapping binding sites of the frataxin homologue assembly factor and
RT the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster
RT scaffold protein.";
RL J. Biol. Chem. 289:30268-30278(2014).
RN [20]
RP FUNCTION.
RX PubMed=25358379; DOI=10.1038/ncomms6013;
RA Webert H., Freibert S.A., Gallo A., Heidenreich T., Linne U., Amlacher S.,
RA Hurt E., Muehlenhoff U., Banci L., Lill R.;
RT "Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1
RT reveals the involvement of ferredoxin.";
RL Nat. Commun. 5:5013-5013(2014).
RN [21]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF MET-141.
RX PubMed=31040179; DOI=10.1074/jbc.ra119.008600;
RA Pandey A.K., Pain J., Dancis A., Pain D.;
RT "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm
RT for iron-sulfur cluster assembly and tRNA thiolation in yeast.";
RL J. Biol. Chem. 294:9489-9502(2019).
RN [22]
RP 3D-STRUCTURE MODELING OF INTERACTION WITH JAC1.
RX PubMed=25973573; DOI=10.1002/prot.24824;
RA Mozolewska M.A., Krupa P., Scheraga H.A., Liwo A.;
RT "Molecular modeling of the binding modes of the iron-sulfur protein to the
RT Jac1 co-chaperone from Saccharomyces cerevisiae by all-atom and coarse-
RT grained approaches.";
RL Proteins 83:1414-1426(2015).
CC -!- FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur
CC (Fe-S) clusters within mitochondria, which is required for maturation
CC of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins.
CC First, a [2Fe-2S] cluster is transiently assembled on the scaffold
CC proteins ISU1 and ISU2. In a second step, the cluster is released from
CC ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation
CC of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters
CC and their target-specific insertion into the recipient apoproteins.
CC Cluster assembly on ISU1/ISU2 depends on the function of the cysteine
CC desulfurase complex NFS1-ISD11, which serves as the sulfur donor for
CC cluster synthesis, the iron-binding protein frataxin (YFH1) as the
CC putative iron donor, and the electron transfer chain comprised of
CC ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their
CC electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by
CC interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like
CC co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the
CC major isoform in yeast, while ISU2 is not detectable in cells grown to
CC stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370,
CC PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440,
CC PubMed:25358379). Also involved in production of a sulfur precursor
CC required for thiolation of cytoplasmic tRNAs (PubMed:31040179).
CC {ECO:0000269|PubMed:10588895, ECO:0000269|PubMed:12970193,
CC ECO:0000269|PubMed:14741370, ECO:0000269|PubMed:15123690,
CC ECO:0000269|PubMed:16341089, ECO:0000269|PubMed:16431909,
CC ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:25358379,
CC ECO:0000269|PubMed:31040179}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:23615440, ECO:0000305|PubMed:12970193};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q9UTC6};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000269|PubMed:10588895, ECO:0000269|PubMed:15123690,
CC ECO:0000269|PubMed:15143178, ECO:0000269|PubMed:16431909}.
CC -!- SUBUNIT: Component of the core Fe-S cluster (ISC) assembly machinery.
CC Interacts with frataxin (PubMed:14741370, PubMed:12947415,
CC PubMed:20815377, PubMed:25228696). Interacts with the mitochondrial co-
CC chaperones JAC1 and SSQ1 (PubMed:12756240, PubMed:15123690,
CC PubMed:22306468, PubMed:23946486, PubMed:23615440). Interacts with NFS1
CC (PubMed:23946486, PubMed:25228696). Interacts with ferredoxin YAH1;
CC interacts with the reduced form (PubMed:25358379).
CC {ECO:0000269|PubMed:12756240, ECO:0000269|PubMed:12947415,
CC ECO:0000269|PubMed:14741370, ECO:0000269|PubMed:15123690,
CC ECO:0000269|PubMed:20815377, ECO:0000269|PubMed:22306468,
CC ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:23946486,
CC ECO:0000269|PubMed:25228696, ECO:0000269|PubMed:25358379}.
CC -!- INTERACTION:
CC Q03020; P53193: JAC1; NbExp=3; IntAct=EBI-29901, EBI-23714;
CC Q03020; P25374: NFS1; NbExp=3; IntAct=EBI-29901, EBI-11991;
CC Q03020; Q05931: SSQ1; NbExp=4; IntAct=EBI-29901, EBI-35227;
CC Q03020; Q07540: YFH1; NbExp=4; IntAct=EBI-29901, EBI-2206814;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10468587, ECO:0000269|PubMed:10588895,
CC ECO:0000269|PubMed:15143178, ECO:0000269|PubMed:16823961}.
CC -!- DISRUPTION PHENOTYPE: Cells deleted for both ISU1 and ISU2 have
CC decreased activity of several respiratory enzymes that contain Fe-S
CC clusters. As a result, cells grow poorly on carbon sources requiring
CC respiration and also accumulate abnormally high levels of iron in their
CC mitochondria. Knockdown of ISU1 in ISU2 knockout cells decreases
CC cytosolic tRNA thiolation, and increases association between SSQ1 and
CC GRX5 (PubMed:31040179, PubMed:23615440). {ECO:0000269|PubMed:10468587,
CC ECO:0000269|PubMed:10588895, ECO:0000269|PubMed:23615440,
CC ECO:0000269|PubMed:31040179}.
CC -!- MISCELLANEOUS: Present with 10800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; U43703; AAB68224.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11298.1; -; Genomic_DNA.
DR PIR; S69049; S69049.
DR RefSeq; NP_015190.1; NM_001183949.1.
DR PDB; 5T0V; EM; 17.50 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x=28-165.
DR PDB; 5TRE; EM; 15.60 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x=28-165.
DR PDBsum; 5T0V; -.
DR PDBsum; 5TRE; -.
DR AlphaFoldDB; Q03020; -.
DR SMR; Q03020; -.
DR BioGRID; 36046; 254.
DR ComplexPortal; CPX-392; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR DIP; DIP-6556N; -.
DR IntAct; Q03020; 11.
DR MINT; Q03020; -.
DR STRING; 4932.YPL135W; -.
DR MaxQB; Q03020; -.
DR PaxDb; Q03020; -.
DR PRIDE; Q03020; -.
DR DNASU; 855968; -.
DR EnsemblFungi; YPL135W_mRNA; YPL135W; YPL135W.
DR GeneID; 855968; -.
DR KEGG; sce:YPL135W; -.
DR SGD; S000006056; ISU1.
DR VEuPathDB; FungiDB:YPL135W; -.
DR eggNOG; KOG3361; Eukaryota.
DR GeneTree; ENSGT00390000015813; -.
DR HOGENOM; CLU_079283_5_0_1; -.
DR InParanoid; Q03020; -.
DR OMA; YKNPRNY; -.
DR BioCyc; MetaCyc:G3O-34034-MON; -.
DR BioCyc; YEAST:G3O-34034-MON; -.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR UniPathway; UPA00266; -.
DR PRO; PR:Q03020; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03020; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; HDA:SGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0008198; F:ferrous iron binding; IDA:SGD.
DR GO; GO:0005506; F:iron ion binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IGI:SGD.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR01999; iscU; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..165
FT /note="Iron sulfur cluster assembly protein 1,
FT mitochondrial"
FT /id="PRO_0000019700"
FT REGION 132..136
FT /note="SSQ1 binding region"
FT /evidence="ECO:0000269|PubMed:15123690"
FT MUTAGEN 63
FT /note="L->S: In ISU1(LVF/SSS); no growth and abolishes
FT interaction with both JAC1 and NFS1; when associated with
FT S-72 and S-94."
FT /evidence="ECO:0000269|PubMed:10588895"
FT MUTAGEN 69
FT /note="C->A: Fails to complement an isu1 deletion
FT mutation."
FT /evidence="ECO:0000269|PubMed:10588895"
FT MUTAGEN 72
FT /note="V->S: In ISU1(LVF/SSS); no growth and abolishes
FT interaction with both JAC1 and NFS1; when associated with
FT S-63 and S-94."
FT /evidence="ECO:0000269|PubMed:10588895"
FT MUTAGEN 94
FT /note="F->S: In ISU1(LVF/SSS); no growth and abolishes
FT interaction with both JAC1 and NFS1; when associated with
FT S-63 and S-72."
FT /evidence="ECO:0000269|PubMed:10588895"
FT MUTAGEN 96
FT /note="C->A: Fails to complement an isu1 deletion
FT mutation."
FT /evidence="ECO:0000269|PubMed:10588895"
FT MUTAGEN 132
FT /note="L->A: No growth."
FT /evidence="ECO:0000269|PubMed:15123690"
FT MUTAGEN 133
FT /note="P->A: Wild-type growth."
FT /evidence="ECO:0000269|PubMed:15123690"
FT MUTAGEN 134..136
FT /note="PVK->AAA: No growth; no interaction with frataxin
FT and SSQ1."
FT /evidence="ECO:0000269|PubMed:15123690,
FT ECO:0000269|PubMed:25228696"
FT MUTAGEN 134
FT /note="P->A: Slow growth; no interaction with SSQ1."
FT /evidence="ECO:0000269|PubMed:15123690"
FT MUTAGEN 135
FT /note="V->A: Wild-type growth; no interaction with SSQ1."
FT /evidence="ECO:0000269|PubMed:15123690"
FT MUTAGEN 136
FT /note="K->A: No growth; no interaction with SSQ1."
FT /evidence="ECO:0000269|PubMed:15123690"
FT MUTAGEN 139
FT /note="C->A: Fails to complement an isu1 deletion
FT mutation."
FT /evidence="ECO:0000269|PubMed:10588895"
FT MUTAGEN 141
FT /note="M->E: Disrupts iron-sulfur (Fe-S) cluster assembly."
FT /evidence="ECO:0000269|PubMed:31040179"
SQ SEQUENCE 165 AA; 17895 MW; E240845A27D2E9EE CRC64;
MLPVITRFAR PALMAIRPVN AMGVLRASSI TKRLYHPKVI EHYTHPRNVG SLDKKLPNVG
TGLVGAPACG DVMRLQIKVN DSTGVIEDVK FKTFGCGSAI ASSSYMTELV QGMTLDDAAK
IKNTEIAKEL SLPPVKLHCS MLAEDAIKAA IKDYKSKRNT PTMLS
