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Literature DB >> 19393741

Protein folding in Escherichia coli: the chaperonin GroE and its substrates.

Millicent Masters¹, Garry Blakely, Andrew Coulson, Neil McLennan, Vollodymyr Yerko, John Acord.

Abstract

A brief summary of the role of DnaK and GroE chaperones in protein folding precedes a discussion of the role of GroE in Escherichia coli. We consider its obligate substrates, the 8 that are both obligate and essential, and the prospects for constructing a mutant that could survive without it. Structural features of GroE-dependent polypeptides are also considered.

Entities: Gene Species

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Year: 2009 PMID： 19393741 DOI： 10.1016/j.resmic.2009.04.002

Source DB: PubMed Journal: Res Microbiol ISSN： 0923-2508 Impact factor: 3.992

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Cited

12 in total

1. A systematic survey of in vivo obligate chaperonin-dependent substrates.

Authors: Kei Fujiwara; Yasushi Ishihama; Kenji Nakahigashi; Tomoyoshi Soga; Hideki Taguchi
Journal: EMBO J Date: 2010-04-01 Impact factor: 11.598

2. Global analysis of chaperone effects using a reconstituted cell-free translation system.

Authors: Tatsuya Niwa; Takashi Kanamori; Takuya Ueda; Hideki Taguchi
Journal: Proc Natl Acad Sci U S A Date: 2012-05-21 Impact factor: 11.205

3. Hyperosmotic stress response of Campylobacter jejuni.

Authors: Andrew Cameron; Emilisa Frirdich; Steven Huynh; Craig T Parker; Erin C Gaynor
Journal: J Bacteriol Date: 2012-09-07 Impact factor: 3.490

4. Conversion of a chaperonin GroEL-independent protein into an obligate substrate.

Authors: Takuya Ishimoto; Kei Fujiwara; Tatsuya Niwa; Hideki Taguchi
Journal: J Biol Chem Date: 2014-10-06 Impact factor: 5.157

5. The Chaperonin GroESL Facilitates Caulobacter crescentus Cell Division by Supporting the Functions of the Z-Ring Regulators FtsA and FzlA.

Authors: Kristen Schroeder; Kristina Heinrich; Ines Neuwirth; Kristina Jonas
Journal: mBio Date: 2021-05-04 Impact factor: 7.867

6. Stress response regulators identified through genome-wide transcriptome analysis of the (p)ppGpp-dependent response in Rhizobium etli.

Authors: Maarten Vercruysse; Maarten Fauvart; Ann Jans; Serge Beullens; Kristien Braeken; Lore Cloots; Kristof Engelen; Kathleen Marchal; Jan Michiels
Journal: Genome Biol Date: 2011-02-16 Impact factor: 13.583

Protein folding in Escherichia coli: the chaperonin GroE and its substrates.

1. A systematic survey of in vivo obligate chaperonin-dependent substrates.

2. Global analysis of chaperone effects using a reconstituted cell-free translation system.

3. Hyperosmotic stress response of Campylobacter jejuni.

4. Conversion of a chaperonin GroEL-independent protein into an obligate substrate.

5. The Chaperonin GroESL Facilitates Caulobacter crescentus Cell Division by Supporting the Functions of the Z-Ring Regulators FtsA and FzlA.

6. Stress response regulators identified through genome-wide transcriptome analysis of the (p)ppGpp-dependent response in Rhizobium etli.

Review 7. Chaperoning roles of macromolecules interacting with proteins in vivo.

8. Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.

9. A proteomic investigation of Fusobacterium nucleatum alkaline-induced biofilms.

Review 10. Macromolecule-assisted de novo protein folding.