Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.
about
Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesisInteraction of J-Protein Co-Chaperone Jac1 with Fe–S Scaffold Isu Is Indispensable In Vivo and Conserved in EvolutionJ protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix.Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1pEssential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins.The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteinsThe Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria.An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1.Dual localized AtHscB involved in iron sulfur protein biogenesis in ArabidopsisAssessment of the biological pathways targeted by isocyanate using N-succinimidyl N-methylcarbamate in budding yeast Saccharomyces cerevisiaeCo-evolution-driven switch of J-protein specificity towards an Hsp70 partner.Kinetic and structural characterization of human mortalinFrataxin and mitochondrial FeS cluster biogenesis.Signaling the mitochondrial unfolded protein response.Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold proteinMitochondrial heat shock protein machinery hsp70/hsp40 is indispensable for proper mitochondrial DNA maintenance and replication.Malfunctioning of the iron-sulfur cluster assembly machinery in Saccharomyces cerevisiae produces oxidative stress via an iron-dependent mechanism, causing dysfunction in respiratory complexes.The response to heat shock and oxidative stress in Saccharomyces cerevisiaeKey players and their role during mitochondrial iron-sulfur cluster biosynthesisBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria.Molecular mechanisms of thermal resistance of the insect trypanosomatid Crithidia thermophila.A role for iron-sulfur clusters in the regulation of transcription factor Yap5-dependent high iron transcriptional responses in yeastCongenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9.Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulationHscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions.Posttranslational regulation of the scaffold for Fe-S cluster biogenesis, Isu.Binding of the chaperone Jac1 protein and cysteine desulfurase Nfs1 to the iron-sulfur cluster scaffold Isu protein is mutually exclusive.Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein-Protein InteractionMitochondrial quality control and communications with the nucleus are important in maintaining mitochondrial function and cell health.Posttranslational control of the scaffold for Fe-S cluster biogenesis as a compensatory regulatory mechanism.Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system.The human escort protein Hep binds to the ATPase domain of mitochondrial hsp70 and regulates ATP hydrolysis.Evolutionary conservation and in vitro reconstitution of microsporidian iron-sulfur cluster biosynthesis.Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae.The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1.The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.The Rieske Iron-Sulfur Protein: Import and Assembly into the Cytochrome bc(1) Complex of Yeast Mitochondria.
P2860
Q24293446-4DE0F927-CF19-49B7-A161-3D3733D63FFAQ27677058-3F031ABD-22C8-4AD5-9E43-EB94724ACE7AQ27930249-08AE488E-370A-446C-B200-8B16DA2D30E0Q27931231-82FFB2E5-2258-4DAF-AE5C-C4A60C88E32CQ27934369-E3E57699-D8C4-4792-A07F-EE22DC6B29EAQ27937038-5D93F6DB-5533-45AA-973C-2F221F899423Q27938366-B8AF57EA-C807-4E64-9A7C-1E7CD077304FQ27939048-122751D8-E546-45D8-85AD-6A8B2964BF64Q28471663-F7F94280-92B9-4CF5-97D0-CC95110BD232Q28541434-9337F367-D261-4A5B-B2A4-DD2BF905A6EDQ33845792-6A6AE5E9-8C54-42E6-A30D-ABD770BFD264Q33919575-973A25C4-60B3-4E1B-8ACA-FC4E8F59A37BQ34094277-F7FC7480-9E98-473B-8DCD-8115FD4D2338Q34263419-9F336947-6884-4C0E-AB38-CE266D57574AQ34430900-0B39444A-AC50-42A4-8B5D-21AF401D0A7FQ35111143-57B59EC5-5BBE-4429-A91F-2E83AE92FE96Q35377490-84C71029-0FB4-442E-AE59-809BE74435EDQ35863026-B0C2FB63-9ED5-4D0B-A245-1CB2D6094BC7Q36005200-24CF2645-C7AA-4351-9B29-D628B34A682BQ36023274-6D11E918-CCE8-4994-AAF3-93B45F12560CQ36291154-8116B038-1046-45D0-A069-86CCA370DB65Q36318429-AF09E2D4-C236-4487-8080-B1AEF6EB6D50Q36318684-E7D81757-D0F6-49D0-A885-5D8AB6979875Q36382196-491E9388-C196-4428-939C-88DC78B7DD6DQ36746171-4D7D5E71-A18E-490F-B461-298D8ED3A0C1Q36843961-9AD657ED-18BB-419B-B290-F3C3C7C21688Q36962268-1592D7CF-67CC-4257-9696-A9754FDD84AFQ36992869-AB7815FC-7FAE-4F26-85D3-206FFCCE9C1FQ37213932-7460BE56-0F78-414D-9365-C8904C8E9469Q37229435-EF8BA831-572C-4E34-BA00-A8AFB9553E85Q37673241-948035C3-9B48-4D1E-A6C8-5DA5E5FE1499Q38849570-D7A112E8-80C0-4C0E-A16D-DB418FD0724FQ39502948-62B07683-5EAD-45B7-B056-0D7326D9BEE6Q40419483-33E84006-0EBD-4646-A0D5-C9AFFFCDADB0Q40832998-7B5768ED-0E39-4408-BDA2-1366B44E31F5Q41836189-49BDE1DF-410F-43AC-948E-927CE358770BQ41895199-6BB85DB4-F385-41AB-A644-B7BE31B349A8Q42065903-FC80C787-F557-45F9-99C5-37816B9A4C61Q42153817-C9C1852F-51D8-48C5-9691-690FDC333885Q42287809-F088E233-EC1E-4A06-8BAC-D9520C3F1572
P2860
Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@ast
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@en
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@nl
type
label
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@ast
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@en
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@nl
prefLabel
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@ast
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@en
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@nl
P2093
P2860
P356
P1476
Ssq1, a mitochondrial Hsp70 in ...... rom its bacterial counterpart.
@en
P2093
Brenda Schilke
Elizabeth A Craig
Helena Knieszner
Jaroslaw Marszalek
Rafal Dutkiewicz
William Walter
P2860
P304
P356
10.1074/JBC.M303527200
P407
P577
2003-08-08T00:00:00Z