Cyclin A-Cys41 does not undergo cell cycle-dependent degradation in Xenopus extracts.
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).
Lorca
T
T
CNRS UPR 8402, Montpellier, France.
Devault
A
A
Colas
P
P
Van Loon
A
A
Fesquet
D
D
Lazaro
J B
JB
Dorée
M
M
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002413:Cations, Divalent; D002453:Cell Cycle; D016213:Cyclins / Q000235:genetics / Q000378:metabolism*; D003545:Cysteine / Q000235:genetics / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D006656:Protamine Kinase / Q000378:metabolism; D014981:Xenopus / Q000378:metabolism*
D002413:Cations, Divalent; D016213:Cyclins; D000255:Adenosine Triphosphate; D006656:Protamine Kinase; D008274:Magnesium; D003545:Cysteine