Antibody characterisation of two distinct conformations of the chaperonin‐containing TCP‐1 from mouse testis

23 January 1995

journal article
Published by Wiley in FEBS Letters

Vol. 358 (2) , 129-132
https://doi.org/10.1016/0014-5793(94)01408-s

Abstract

We describe a panel of antibodies specific to individual subunits of the chaperonin-containing TCP-1 (CCT) and one antibody that reacts with all the subunits of CCT. Immunoblot analysis of CCT purified from mouse testis suggests that the testis-specific subunit, S6, may be related to CCTζ and that a co-purifying 63 kDa protein may be a novel subunit of CCT. Using these antibodies in the analysis of CCT subjected to non-denaturing IEF we observed the resolution of two distinct conformations of CCT, which differ in their susceptibility to proteolysis and in the number of associated polypeptides

Keywords

This publication has 14 references indexed in Scilit:

Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
Trends in Biochemical Sciences, 1994
Residues in chaperonin GroEL required for polypeptide binding and release
Nature, 1994
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Nature, 1994
Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
Nature, 1994
A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle.
The Journal of cell biology, 1994
Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
Current Biology, 1994
Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin
The Journal of cell biology, 1993
ATP induces large quaternary rearrangements in a cage-like chaperonin structure
Current Biology, 1993
TCP1 complex is a molecular chaperone in tubulin biogenesis
Nature, 1992
A cytoplasmic chaperonin that catalyzes β-actin folding
Published by Elsevier ,1992