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Cell. 1992 Jun 12;69(6):1043-50.

A cytoplasmic chaperonin that catalyzes beta-actin folding.

Author information

1
Department of Biochemistry, New York University Medical Center, New York 10016.

Abstract

We have isolated a cytoplasmic chaperonin based on its ability to catalyze the folding of denatured beta-actin. The cytoplasmic chaperonin is organized as a multisubunit toroid and requires Mg2+ and ATP for activity. The folding reaction proceeds via the rapid ATP-independent formation of a binary complex, followed by a slower ATP-dependent release of the native product. Electron microscopic observations reveal a striking structural change that occurs upon addition of Mg2+ and ATP. The eukaryotic cytoplasm thus contains a chaperonin that is functionally analagous to its prokaryotic, mitochondrial, and chloroplastic counterparts.

PMID:
1351421
DOI:
10.1016/0092-8674(92)90622-j
[Indexed for MEDLINE]

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