Cyclin A-Cys41 does not undergo cell cycle-dependent degradation in Xenopus extracts.

Abstract:

:Truncated cyclin A and cyclin B lacking the N-terminal domain comprising the 'destruction box' escape from proteolysis and arrest cells at metaphase. Mutation of a conserved arginine residue of the destruction domain makes cyclin B resistant to proteolysis. Here we show that mutation of the same residue also makes cyclin A resistant to proteolysis, in either of two situations in which the cyclin degradation pathway is turned on: (i) in Xenopus extracts of activated eggs where the degradation pathway has been permanently turned on by adding a recombinant undegradable cyclin B in which the arginine residue of the destruction box has been substituted by alanine; (ii) in extracts of metaphase II-arrested oocytes after Ca(2+)-dependent inactivation of the cytostatic factor (CSF).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lorca T,Devault A,Colas P,Van Loon A,Fesquet D,Lazaro JB,Dorée M

doi

10.1016/0014-5793(92)80844-7

keywords:

subject

Has Abstract

pub_date

1992-07-13 00:00:00

pages

90-3

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80844-7

journal_volume

306

pub_type

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