The Cdk-activating kinase (CAK) from budding yeast.

Abstract:

:Activation of the cyclin-dependent kinases to promote cell cycle progression requires their association with cyclins as well as phosphorylation of a threonine (residue 161 in human p34cdc2). This phosphorylation is carried out by CAK, the Cdk-activating kinase. We have purified and cloned CAK from S. cerevisiae. Unlike CAKs from other organisms, Cak1p is active as a monomer, has full activity when expressed in E. coli, and is not a component of the basal transcription factor, TFIIH. A temperature-sensitive mutation in CAK1 confers a G2 delay accompanied by low Cdc28p protein kinase activity and shows genetic interactions with altered expression of the gene for the major mitotic cyclin, CLB2. Our data raise the intriguing possibility that p40MO15-cyclin H-MAT1, identified as the predominant CAK in vertebrate cell extracts, may not function as a physiological CAK.

journal_name

Cell

journal_title

Cell

authors

Kaldis P,Sutton A,Solomon MJ

doi

10.1016/s0092-8674(00)80129-4

subject

Has Abstract

pub_date

1996-08-23 00:00:00

pages

553-64

issue

4

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)80129-4

journal_volume

86

pub_type

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