Loading…

ATP-Induced Allostery in the Eukaryotic Chaperonin CCT Is Abolished by the Mutation G345D in CCT4 that Renders Yeast Temperature-Sensitive for Growth

Saccharomyces cerevisiae yeast cells containing the chaperonin CCT (chaperonin-containing t-complex polypeptide 1 (TCP-1)) with the G345D mutation in subunit CCT4 (anc2-1) are temperature-sensitive for growth and display defects in organization of actin structure, budding and cell shape. In this fir...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular biology 2008-03, Vol.377 (2), p.469-477
Main Authors: Shimon, Liat, Hynes, Gillian M., McCormack, Elizabeth A., Willison, Keith R., Horovitz, Amnon
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Saccharomyces cerevisiae yeast cells containing the chaperonin CCT (chaperonin-containing t-complex polypeptide 1 (TCP-1)) with the G345D mutation in subunit CCT4 (anc2-1) are temperature-sensitive for growth and display defects in organization of actin structure, budding and cell shape. In this first structure–function analysis of CCT, we show that this mutation abolishes both intra- and inter-ring cooperativity in ATP binding by CCT. The finding that a single mutation in only one subunit in each CCT ring has such drastic effects highlights the importance of allostery for its in vivo function. These results, together with other kinetic data for wild-type CCT reported in this study, provide support for the sequential model for ATP-dependent allosteric transitions in CCT.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2008.01.011