Literature DB >> 2897629

Homologous plant and bacterial proteins chaperone oligomeric protein assembly.

S M Hemmingsen1, C Woolford, S M van der Vies, K Tilly, D T Dennis, C P Georgopoulos, R W Hendrix, R J Ellis.   

Abstract

An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants. The product of the Escherichia coli groEL gene is essential for cell viability and is required for the assembly of bacteriophage capsids. Sequencing of the groEL gene and the complementary cDNA encoding the chloroplast protein has revealed that these proteins are evolutionary homologues which we term 'chaperonins'. Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes. Assisted post-translational assembly of oligomeric protein structures is emerging as a general cellular phenomenon.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 2897629     DOI: 10.1038/333330a0

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


  357 in total

Review 1.  Assembly of chaperonin complexes.

Authors:  A R Kusmierczyk; J Martin
Journal:  Mol Biotechnol       Date:  2001-10       Impact factor: 2.695

2.  Arabidopsis thaliana type I and II chaperonins.

Authors:  J E Hill; S M Hemmingsen
Journal:  Cell Stress Chaperones       Date:  2001-07       Impact factor: 3.667

3.  Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10.

Authors:  Chris Walters; Neil Errington; Arther J Rowe; Stephen E Harding
Journal:  Biochem J       Date:  2002-06-15       Impact factor: 3.857

4.  GroEL binds a late folding intermediate of phage P22 coat protein.

Authors:  M D de Beus; S M Doyle; C M Teschke
Journal:  Cell Stress Chaperones       Date:  2000-07       Impact factor: 3.667

Review 5.  An emerging concept of prion infections as a form of transmissible cerebral amyloidosis.

Authors:  Omar Lupi; Marcius Achiame Peryassu
Journal:  Prion       Date:  2007 Oct-Dec       Impact factor: 3.931

6.  Identifying natural substrates for chaperonins using a sequence-based approach.

Authors:  George Stan; Bernard R Brooks; George H Lorimer; D Thirumalai
Journal:  Protein Sci       Date:  2004-12-02       Impact factor: 6.725

7.  Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli.

Authors:  J Zeilstra-Ryalls; O Fayet; C Georgopoulos
Journal:  J Bacteriol       Date:  1994-11       Impact factor: 3.490

8.  Bacterial heat shock proteins directly induce cytokine mRNA and interleukin-1 secretion in macrophage cultures.

Authors:  C Retzlaff; Y Yamamoto; P S Hoffman; H Friedman; T W Klein
Journal:  Infect Immun       Date:  1994-12       Impact factor: 3.441

9.  Primary sequence and location of the idiotopes of V-88, a DNA-binding monoclonal autoantibody, determined by idiotope scanning with synthetic peptides on pins.

Authors:  N A Staines; F J Ward; A N Denbury; J Mitchiner; O Hartley; D Eilat; D A Isenberg; S Bansal
Journal:  Immunology       Date:  1993-03       Impact factor: 7.397

10.  Mycobacterium tuberculosis expresses two chaperonin-60 homologs.

Authors:  T H Kong; A R Coates; P D Butcher; C J Hickman; T M Shinnick
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-01       Impact factor: 11.205

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.