PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15123690-1 2004 Isu, the scaffold for assembly of Fe-S clusters in the yeast mitochondrial matrix, is a substrate protein for the Hsp70 Ssq1 and the J-protein Jac1 in vitro. Iron 34-38 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 120-124 15123690-5 2004 We conclude that the Ssq1-Isu substrate interaction is critical for Fe-S cluster biogenesis in vivo. Iron 68-72 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 21-25 12970193-4 2003 In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins. Iron 135-137 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 46-51 11278728-2 2001 We have previously isolated yeast mutants of the mitochondrial Hsp70, Ssq1p, in a genetic screen for mutants with altered iron homeostasis. Iron 122-126 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 70-75 11950925-3 2002 Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression of SSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Iron 158-162 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 91-95 11689493-7 2001 JAC1, an ortholog of hscB, and SSQ1, a paralog of hscA, have been shown to be required for iron-sulfur cluster assembly in mitochondria of Saccharomyces cerevisiae. Iron 91-95 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 31-35 11278728-11 2001 Similar mitochondrial localization and similar mutant phenotypes suggest that Ssq1p and Jac1p are functional partners in iron homeostasis. Iron 121-125 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 78-83 11273703-6 2001 Mutants in Ssq1 were reported to have low levels of iron sulfur (FeS) cluster-containing enzymes. Iron 65-68 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 11-15 9813017-8 1998 Homologues of Ssq1p and Jac1p are found in bacteria in close association with genes proposed to be involved in iron-sulfur protein biosynthesis. Iron 111-115 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 14-19 11171977-1 2001 A minor Hsp70 chaperone of the mitochondrial matrix of Saccharomyces cerevisiae, Ssq1, is involved in the formation or repair of Fe/S clusters and/or mitochondrial iron metabolism. Iron 129-131 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 81-85 11171977-1 2001 A minor Hsp70 chaperone of the mitochondrial matrix of Saccharomyces cerevisiae, Ssq1, is involved in the formation or repair of Fe/S clusters and/or mitochondrial iron metabolism. Iron 164-168 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 81-85 11171977-4 2001 Fe/S enzyme activities remain low in both jac1 and ssq1 mutant mitochondria even if normal mitochondrial iron levels are maintained. Iron 105-109 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 51-55 9813017-12 1998 Taken together these results suggest a role for Ssq1p, Jac1p, and Nfs1p in assembly/maturation of mitochondrial iron-sulfur proteins and that one or more of the target Fe/S proteins contribute to oxidative damage in cells lacking copper/zinc SOD. Iron 112-116 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 48-53 20224575-3 2010 Here, we report that existence of the Hsp70 Ssq1, which arose by duplication of the gene encoding multifunction mtHsp70 and specializes in iron-sulphur cluster biogenesis, correlates with functional and structural changes in the J domain of its J-protein partner Jac1. Iron 139-143 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 44-48 25462017-2 2014 Both genes are homologs of the Ssq1 gene involved in Fe-S cluster assembly in yeast. Iron 53-57 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 31-35 9660806-0 1998 Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. Iron 85-89 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 18-23 9660806-1 1998 Here we show that the yeast mitochondrial chaperone Ssc2p, a homolog of mt-Hsp70, plays a critical role in mitochondrial iron homeostasis. Iron 121-125 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 52-57 31040179-5 2019 The mitochondrial biosynthesis of (Fe-S)int required ISC components such as Nfs1 cysteine desulfurase, Isu1/2 scaffold, and Ssq1 chaperone. Iron 35-39 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 124-128 28720726-4 2017 Iron metabolism and, more particularly, Fe-S cluster formation are involved in regulating this process, since the responsible Hsp70 chaperone, Ssq1, is required. Iron 0-4 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 143-147 28720726-4 2017 Iron metabolism and, more particularly, Fe-S cluster formation are involved in regulating this process, since the responsible Hsp70 chaperone, Ssq1, is required. Iron 40-44 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 143-147 25356756-7 2014 Raman spectroscopy analysis and immunoblotting indicated that in mitochondria from SSQ1 and ISA1 mutants, the content of [Fe-S] centers was decreased, as was formation of Rieske protein-dependent supercomplex III2IV2, but this was not observed in the iron-deficient ATX1 and MRS4 mutants. Iron 251-255 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 83-87 22915593-2 2012 Using a genetic screen to identify genes involved in Yap5 iron sensing, we discovered that a mutation in SSQ1, which encodes a mitochondrial chaperone involved in iron-sulfur cluster synthesis, prevented expression of Yap5 target genes. Iron 58-62 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 105-109 22915593-2 2012 Using a genetic screen to identify genes involved in Yap5 iron sensing, we discovered that a mutation in SSQ1, which encodes a mitochondrial chaperone involved in iron-sulfur cluster synthesis, prevented expression of Yap5 target genes. Iron 163-167 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 105-109 15958384-0 2005 Compensation for a defective interaction of the hsp70 ssq1 with the mitochondrial Fe-S cluster scaffold isu. Iron 82-86 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 54-58 17331979-3 2007 One interactor was mortalin/GRP75, a homolog of the yeast ssq1 chaperone that integrates iron-sulfur clusters into imported mitochondrial proteins. Iron 89-93 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 58-62 17453917-0 2007 Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Iron 64-68 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 26-30 16601688-4 2006 The bulk of mitochondrial iron is normally unavailable to SOD2, but when mitochondrial iron homeostasis is disrupted, for example, by mutations in S. cerevisiae mtm1, ssq1 and grx5, iron accumulates in a reactive form that potently competes with manganese for binding to SOD2, inactivating the enzyme. Iron 26-30 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 167-171 16601688-4 2006 The bulk of mitochondrial iron is normally unavailable to SOD2, but when mitochondrial iron homeostasis is disrupted, for example, by mutations in S. cerevisiae mtm1, ssq1 and grx5, iron accumulates in a reactive form that potently competes with manganese for binding to SOD2, inactivating the enzyme. Iron 87-91 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 167-171 16601688-4 2006 The bulk of mitochondrial iron is normally unavailable to SOD2, but when mitochondrial iron homeostasis is disrupted, for example, by mutations in S. cerevisiae mtm1, ssq1 and grx5, iron accumulates in a reactive form that potently competes with manganese for binding to SOD2, inactivating the enzyme. Iron 87-91 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 167-171 16431909-1 2006 The specialized yeast mitochondrial chaperone system, composed of the Hsp70 Ssq1p, its co-chaperone J-protein Jac1p, and the nucleotide release factor Mge1p, perform a critical function in the biogenesis of iron-sulfur (Fe/S) proteins. Iron 220-222 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 76-81 19561359-2 2009 Although mitochondrial iron does not normally bind SOD2, iron will misincorporate into Saccharomyces cerevisiae Sod2p when cells are starved for manganese or when mitochondrial iron homeostasis is disrupted by mutations in yeast grx5, ssq1, and mtm1. Iron 57-61 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 235-239 19561359-2 2009 Although mitochondrial iron does not normally bind SOD2, iron will misincorporate into Saccharomyces cerevisiae Sod2p when cells are starved for manganese or when mitochondrial iron homeostasis is disrupted by mutations in yeast grx5, ssq1, and mtm1. Iron 57-61 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 235-239 19561359-6 2009 Iron binds Sod2p in yeast mutants blocking late stages of iron-sulfur cluster biogenesis (grx5, ssq1, and atm1), but not in mutants defective in the upstream Isu proteins that serve as scaffolds for iron-sulfur biosynthesis. Iron 0-4 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 96-100 15958384-1 2005 Ssq1, a specialized yeast mitochondrial Hsp70, plays a critical role in the biogenesis of proteins containing Fe-S clusters through its interaction with Isu, the scaffold on which clusters are built. Iron 110-114 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 0-4 15958384-4 2005 In contrast, cells expressing Ssq1(V472F), whose affinity for Isu is at least 10-fold lower than that of wild-type Ssq1, had only moderately reduced Fe-S enzyme activities and increased iron levels and grew similarly to wild-type cells. Iron 149-151 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 30-35 15958384-4 2005 In contrast, cells expressing Ssq1(V472F), whose affinity for Isu is at least 10-fold lower than that of wild-type Ssq1, had only moderately reduced Fe-S enzyme activities and increased iron levels and grew similarly to wild-type cells. Iron 149-151 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 30-34 15958384-4 2005 In contrast, cells expressing Ssq1(V472F), whose affinity for Isu is at least 10-fold lower than that of wild-type Ssq1, had only moderately reduced Fe-S enzyme activities and increased iron levels and grew similarly to wild-type cells. Iron 186-190 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 30-35 15958384-4 2005 In contrast, cells expressing Ssq1(V472F), whose affinity for Isu is at least 10-fold lower than that of wild-type Ssq1, had only moderately reduced Fe-S enzyme activities and increased iron levels and grew similarly to wild-type cells. Iron 186-190 Hsp70 family ATPase SSQ1 Saccharomyces cerevisiae S288C 30-34