Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

Thomas Langer; Chi Lu; Harrison Echols; John Flanagan; Manajit K. Hayer; F. Ulrich Hartl

doi:10.1038/356683a0

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

Thomas Langer
, Chi Lu
, Harrison Echols
, John Flanagan
, Manajit K. Hayer
, F. Ulrich Hartl

Research output: Contribution to journal › Article › peer-review

904 Scopus citations

Abstract

The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding poly-peptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.

Original language	English (US)
Pages (from-to)	683-689
Number of pages	7
Journal	Nature
Volume	356
Issue number	6371
DOIs	https://doi.org/10.1038/356683a0
State	Published - 1992

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title = "Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding",

abstract = "The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding poly-peptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.",

author = "Thomas Langer and Chi Lu and Harrison Echols and John Flanagan and Hayer, \{Manajit K.\} and Hartl, \{F. Ulrich\}",

year = "1992",

doi = "10.1038/356683a0",

language = "English (US)",

volume = "356",

pages = "683--689",

journal = "Nature",

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T1 - Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

AU - Langer, Thomas

AU - Lu, Chi

AU - Echols, Harrison

AU - Flanagan, John

AU - Hayer, Manajit K.

AU - Hartl, F. Ulrich

PY - 1992

Y1 - 1992

N2 - The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding poly-peptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.

AB - The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding poly-peptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.

UR - https://www.scopus.com/pages/publications/0026596223

UR - https://www.scopus.com/pages/publications/0026596223#tab=citedBy

U2 - 10.1038/356683a0

DO - 10.1038/356683a0

M3 - Article

C2 - 1349157

AN - SCOPUS:0026596223

SN - 0028-0836

VL - 356

SP - 683

EP - 689

JO - Nature

JF - Nature

IS - 6371

ER -

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

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