Specificity of DnaK for arginine/lysine and effect of DnaJ on the amino acid specificity of DnaK. (Q54586686)

1 June 2018

title

Specificity of DnaK for arginine/lysine and effect of DnaJ on the amino acid specificity of DnaK. (English)

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1 June 2018

author name string

de Crouy-Chanel A

series ordinal

1

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1 June 2018

Kohiyama M

series ordinal

2

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1 June 2018

Richarme G

series ordinal

3

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1 June 2018

language of work or name

English

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publication date

1 June 1996

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1 June 2018

Journal of Biological Chemistry

published in

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volume

271

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issue

26

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page(s)

15486-15490

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Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

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The essential Escherichia coli msgB gene, a multicopy suppressor of a temperature-sensitive allele of the heat shock gene grpE, is identical to dapE

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DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli

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Role of heat shock protein DnaK in osmotic adaptation of Escherichia coli

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Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding

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21 January 2018

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Net N-C charge imbalance may be important for signal sequence function in bacteria

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Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

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Peptide binding and release by proteins implicated as catalysts of protein assembly

21 January 2018

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Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure

21 January 2018

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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

21 January 2018

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The hydrophobic nature of GroEL-substrate binding

21 January 2018

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ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.26.15486

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1 June 2018

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1 June 2018