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Literature DB >> 1349157

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

T Langer¹, C Lu, H Echols, J Flanagan, M K Hayer, F U Hartl.

Abstract

The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding polypeptide 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.

Entities: Chemical Gene Species

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Year: 1992 PMID： 1349157 DOI： 10.1038/356683a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

251 in total

1. The substrate binding domain of DnaK facilitates slow protein refolding.

Authors: Naoki Tanaka; Shota Nakao; Hiromasa Wadai; Shoichi Ikeda; Jean Chatellier; Shigeru Kunugi
Journal: Proc Natl Acad Sci U S A Date: 2002-11-14 Impact factor: 11.205

2. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

Authors: M Gautschi; H Lilie; U Fünfschilling; A Mun; S Ross; T Lithgow; P Rücknagel; S Rospert
Journal: Proc Natl Acad Sci U S A Date: 2001-03-27 Impact factor: 11.205

3. What is a co-chaperone?

Authors: Avrom J Caplan
Journal: Cell Stress Chaperones Date: 2003 Impact factor: 3.667

4. Levels of epsilon, an essential replication subunit of Escherichia coli DNA polymerase III, are controlled by heat shock proteins.

Authors: P L Foster; M G Marinus
Journal: J Bacteriol Date: 1992-12 Impact factor: 3.490

5. Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

Authors: A Gragerov; E Nudler; N Komissarova; G A Gaitanaris; M E Gottesman; V Nikiforov
Journal: Proc Natl Acad Sci U S A Date: 1992-11-01 Impact factor: 11.205

6. Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein.

Authors: H J Hoffmann; S K Lyman; C Lu; M A Petit; H Echols
Journal: Proc Natl Acad Sci U S A Date: 1992-12-15 Impact factor: 11.205

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

1. The substrate binding domain of DnaK facilitates slow protein refolding.

2. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

3. What is a co-chaperone?

4. Levels of epsilon, an essential replication subunit of Escherichia coli DNA polymerase III, are controlled by heat shock proteins.

5. Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

6. Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein.

7. Alpha-crystallin can function as a molecular chaperone.

8. Isolation and characterization of point mutations in the Escherichia coli grpE heat shock gene.

Review 9. Translational regulation of the heat shock response.

10. Subcellular localization and chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70.