Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. (Q45107765)

9 December 2017

Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. (English)

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9 December 2017

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Jonathan J Silberg

1

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9 December 2017

Tim L Tapley

series ordinal

2

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9 December 2017

Kevin G Hoff

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3

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9 December 2017

Larry E Vickery

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4

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9 December 2017

language of work or name

English

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publication date

13 October 2004

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Journal of Biological Chemistry

9 December 2017

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9 December 2017

279

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9 December 2017

52

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9 December 2017

53924-53931

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Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli

9 December 2017

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Preferential substrate binding orientation by the molecular chaperone HscA.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Hsp70 chaperone machines.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Role of the J-domain in the cooperation of Hsp40 with Hsp70.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

An improved assay for nanomole amounts of inorganic phosphate

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393–507) in complex with the peptide NRLLLTG

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Structural insights into substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

The second step of ATP binding to DnaK induces peptide release.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

GrpE accelerates peptide binding and release from the high affinity state of DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Feedback regulation of iron-sulfur cluster biosynthesis

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410117200

Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

IscU as a Scaffold for Iron−Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscU†

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410117200

21 January 2018

Identifiers

DOI

10.1074/JBC.M410117200

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9 December 2017

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