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

Détails

ID Serval
serval:BIB_142682713035
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis.
Périodique
Journal of Biological Chemistry
Auteur(s)
Weiss C., Goloubinoff P.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
1995
Volume
270
Numéro
23
Pages
13956-13960
Langue
anglais
Résumé
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.
Mots-clé
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
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 13:42
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