A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis.

Details

Serval ID
serval:BIB_142682713035
Type
Article: article from journal or magazin.
Collection
Publications
Title
A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis.
Journal
Journal of Biological Chemistry
Author(s)
Weiss C., Goloubinoff P.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Publication state
Published
Issued date
1995
Volume
270
Number
23
Pages
13956-13960
Language
english
Abstract
The highly conserved aspartic acid residue at position 87 of the Escherichia coli chaperonin GroEL was mutated to glutamic acid. When expressed in an E. coli groEL mutant strain deficient for phage morphogenesis, plasmid-encoded GroEL mutant D87E restored T4 phage morphogenesis. It did not, however, reactivate the transcription of a recombinant luciferase operon from Vibrio fischeri. In vitro, GroEL mutant D87E was found to be impaired in the ability to bind nonnative proteins and to hydrolyze ATP, resulting in less efficient refolding of urea-denatured ribulose-1,5-bisphosphate carboxylase/oxygenase. Mutant oligomer D87E GroEL14 was able to bind GroES7 as efficiently as wild-type GroEL14. The conserved aspartic acid residue at position 87 located in the equatorial domain of GroEL (Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D.C., Joachimiak, A., Horwich, A.L., and Sigler, P.B. (1994) Nature 371, 578-586) is thus inferred to have a dual effect on the binding of nonnative proteins to the GroEL14 core chaperonin and on ATP hydrolysis.
Keywords
Adenosine Triphosphate/metabolism, Amino Acid Sequence, Base Sequence, Chaperonin 10/metabolism, Chaperonin 60/chemistry, Chaperonin 60/metabolism, Hydrolysis, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Folding, Structure-Activity Relationship
Pubmed
Web of science
Create date
24/01/2008 20:02
Last modification date
20/08/2019 12:42
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