A cdc2-like kinase associated with commitment to division in Paramecium tetraurelia.
Cell division in higher eukaryotes is mainly controlled by p34cdc2 or related kinases and by other components of these kinase complexes. We present evidence that cdc2-like kinases also occur in Paramecium. Two polypeptides reacted with an antibody directed against the perfectly conserved PSTAIR region found in cdc2 kinases in other eukaryotes. Only the less abundant peptide bound to p13suc1 from Schizosaccharomyces pombe. Using centrifugal elutriation to select cells on the basis of size, we isolated highly synchronous Paramecium G1 cells. With this procedure, we demonstrated that the p13suc1-associated cdc2-like histone H1 kinase was activated before cell division at the point of commitment to division in Paramecium. Further, we show that Paramecium cdc2-like proteins occurred principally as monomers and that these monomers were active as histone H1 kinases in vitro.
Tang
L
L
Department of Zoology, University of British Columbia, Vancouver, Canada.
Pelech
S L
SL
Berger
J D
JD
D000595:Amino Acid Sequence; D000818:Animals; D016203:CDC2 Protein Kinase / Q000378:metabolism*; D002453:Cell Cycle; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D016200:Maturation-Promoting Factor / Q000378:metabolism*; D008969:Molecular Sequence Data; D016805:Paramecium tetraurelia / Q000201:enzymology* / Q000254:growth & development
D016203:CDC2 Protein Kinase; D016200:Maturation-Promoting Factor