Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed (Q47765907)

5 February 2018

title

Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed (English)

1 reference

5 February 2018

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Pierre Genevaux

4

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Manajit Hayer-Hartl

object named as

Manajit Hayer-Hartl

5

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Franz-Ulrich Hartl

8

object named as

F Ulrich Hartl

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5 February 2018

Vishwas R Agashe

1

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5 February 2018

Suranjana Guha

2

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5 February 2018

Hung-Chun Chang

3

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5 February 2018

Markus Stemp

6

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5 February 2018

Costa Georgopoulos

7

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5 February 2018

José M Barral

9

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5 February 2018

language of work or name

English

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publication date

1 April 2004

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5 February 2018

published in

Cell

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5 February 2018

volume

117

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5 February 2018

issue

2

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5 February 2018

page(s)

199-209

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5 February 2018

Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase

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Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor

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Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

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The Hsp70 and Hsp60 chaperone machines

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Getting newly synthesized proteins into shape.

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A set of pBR322-compatible plasmids allowing the testing of chaperone-assisted folding of proteins overexpressed in Escherichia coli

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Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes

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Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

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Folding of newly translated proteins in vivo: the role of molecular chaperones

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

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Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase

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In vivo analysis of the overlapping functions of DnaK and trigger factor

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Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase

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Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli

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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

The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes.

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Three-dimensional structure of beta-galactosidase from E. coli

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Folding of firefly luciferase during translation in a cell-free system.

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L23 protein functions as a chaperone docking site on the ribosome

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7 January 2021

The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane

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7 January 2021

Interaction of trigger factor with the ribosome

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7 January 2021

Recombination of protein domains facilitated by co-translational folding in eukaryotes.

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7 January 2021

Folding and association of beta-Galactosidase

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Co-translational folding of an alphavirus capsid protein in the cytosol of living cells

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7 January 2021

Binding specificity of Escherichia coli trigger factor

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7 January 2021

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.

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

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7 January 2021

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor

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7 January 2021

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

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

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7 January 2021

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

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7 January 2021

10.1016/S0092-8674(04)00299-5

Identifiers

DOI

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5 February 2018

1 reference

5 February 2018