Mutational Screen Identifies Critical Amino Acid Residues of β-Actin Mediating Interaction between Its Folding Intermediates and Eukaryotic Cytosolic Chaperonin CCT-Reference-Cited by-同舟云学术

Mutational Screen Identifies Critical Amino Acid Residues of β-Actin Mediating Interaction between Its Folding Intermediates and Eukaryotic Cytosolic Chaperonin CCT

Published:2001-08 Issue:2 Volume:135 Page:185-197
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

McCormack Elizabeth A.,Rohman Mattias J.,Willison Keith R.

Publisher

Elsevier BV

Subject

Structural Biology

Reference26 articles.

1. Mapping the binding site of thymosin beta4 on actin by competition with G-actin binding proteins indicates negative co-operativity between binding sites located on opposite subdomains of actin;Ballweber;Biochem. J.,1997

2. Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein;Field;Cell,1990

3. An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein;Freeman;J. Biol. Chem.,1995

4. ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast;Gieselmann;FEBS Lett.,1992

5. Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding;Grantham;J. Biol. Chem.,2000

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