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A chaperone with a hydrophilic surface.

N J Cowan¹, S A Lewis

¹Department of Biochemistry, New York University Medical Center, 550 First Avenue, New York, New York 10016, USA. cowann01@mcrcr.med.nyu.edu

Nature Structural Biology

|December 14, 1999

Summary

This summary is machine-generated.

Tubulin folding requires multiple chaperone proteins. The yeast cofactor A homolog, Rbl2p, forms a dimer with hydrophilic surfaces, interacting with partially folded beta-tubulin.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Tubulin is a key component of microtubules, essential for cell structure and division.
The proper folding of tubulin is a complex process mediated by multiple chaperone proteins.
Seven chaperones, including prefoldin, CCT, and tubulin-specific cofactors A-E, are involved in native tubulin folding.