Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains (Q77918974)

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9 December 2019

title

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains (English)

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9 December 2019

author name string

S A Teter

1

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9 December 2019

W A Houry

2

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9 December 2019

D Ang

3

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9 December 2019

T Tradler

4

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9 December 2019

D Rockabrand

5

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9 December 2019

G Fischer

6

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9 December 2019

P Blum

7

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9 December 2019

C Georgopoulos

8

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9 December 2019

F U Hartl

9

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9 December 2019

language of work or name

English

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publication date

1 June 1999

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9 December 2019

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9 December 2019

volume

97

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9 December 2019

issue

6

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9 December 2019

page(s)

755-765

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The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds

9 December 2019

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Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

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Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

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The 70-kDa heat-shock protein/DnaK chaperone system is required for the productive folding of ribulose-biphosphate carboxylase subunits in Escherichia coli

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In vivo observation of polypeptide flux through the bacterial chaperonin system.

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

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Role of the major heat shock proteins as molecular chaperones

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Protein folding in the cell

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Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.

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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

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7 January 2021

Functional specificity among Hsp70 molecular chaperones

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Protein folding in vivo: unraveling complex pathways

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Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures

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7 January 2021

Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides

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7 January 2021

Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation

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7 January 2021

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7 January 2021

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Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

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7 January 2021

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Identifiers

DOI

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9 December 2019

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