Publication Date:
1994-07-29
Description:
The particular structural arrangement of chaperonins probably contributes to their ability to assist in the folding of proteins. The interaction of the oligomeric bacterial chaperonin GroEL and its cochaperonin, GroES, in the presence of adenosine diphosphate (ADP) forms an asymmetric complex. However, in the presence of adenosine triphosphate (ATP) or its nonhydrolyzable analogs, symmetric complexes were found by electron microscopy and image analysis. The existence of symmetric chaperonin complexes is not predicted by current models of the functional cycle for GroE-mediated protein folding. Because complete folding of a nonnative substrate protein in the presence of GroEL and GroES only occurs in the presence of ATP, but not with ADP, the symmetric chaperonin complexes formed during the GroE cycle are proposed to be functionally significant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmidt, M -- Rutkat, K -- Rachel, R -- Pfeifer, G -- Jaenicke, R -- Viitanen, P -- Lorimer, G -- Buchner, J -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):656-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7913554" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Diphosphate/pharmacology
;
Adenosine Triphosphatases/metabolism
;
Adenosine Triphosphate/metabolism
;
Bacterial Proteins/*chemistry/metabolism/ultrastructure
;
Biopolymers
;
Chaperonin 10
;
Chaperonin 60
;
Heat-Shock Proteins/*chemistry/metabolism/ultrastructure
;
Hydrolysis
;
Microscopy, Electron
;
Protein Binding
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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