TY - JOUR
T1 - Isolation and characterization of goldfish cdk2, a cognate variant of the cell cycle regulator cdc2
AU - Hirai, T.
AU - Yamashita, M.
AU - Yoshikuni, M.
AU - Tokumoto, T.
AU - Kajiura, H.
AU - Sakai, N.
AU - Nagahama, Y.
N1 - Funding Information:
\Ve thank Professor P. Nurse for providing sion strain of E co/i This work was supported Scientific Research from the Ministry of Education, ture of Japan (0120210 to Y.N.), the Naito Foundation, Health Sciences Foundation. This study was carried NIBB Cooperative Research Program (91-124).
PY - 1992/7
Y1 - 1992/7
N2 - This paper reports the nucleotide and predicted amino acid sequences of the goldfish cdk2, a cognate variant of the cell cycle regulator cdc2. The predicted protein sequence shows strong homology to the other known cdk2 (88% for Xenopus and 90% for human). A monoclonal antibody against the C-terminal sequence of goldfish cdk2 recognized a 34-kDa protein in extracts from various goldfish tissues. The protein level was high in such tissues as testis and ovary containing actively dividing cells. Protein cdk2 binds to p13suc1, the fission yeast suc1+ gene product, but not to cyclin B, with which cdc2 forms a complex. The kinase activity of cdk2 increased 30-fold when oocytes matured, although its protein level did not remarkably change. Anti-cdk2 immunoprecipitates from 32P-labeled mature oocyte extracts contained a 47-kDa protein, which was not recognized by either anti-cyclin A or anti-cyclin B antibody, indicating complex formation of cdk2 with a protein other than cyclins A or B.
AB - This paper reports the nucleotide and predicted amino acid sequences of the goldfish cdk2, a cognate variant of the cell cycle regulator cdc2. The predicted protein sequence shows strong homology to the other known cdk2 (88% for Xenopus and 90% for human). A monoclonal antibody against the C-terminal sequence of goldfish cdk2 recognized a 34-kDa protein in extracts from various goldfish tissues. The protein level was high in such tissues as testis and ovary containing actively dividing cells. Protein cdk2 binds to p13suc1, the fission yeast suc1+ gene product, but not to cyclin B, with which cdc2 forms a complex. The kinase activity of cdk2 increased 30-fold when oocytes matured, although its protein level did not remarkably change. Anti-cdk2 immunoprecipitates from 32P-labeled mature oocyte extracts contained a 47-kDa protein, which was not recognized by either anti-cyclin A or anti-cyclin B antibody, indicating complex formation of cdk2 with a protein other than cyclins A or B.
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U2 - 10.1016/0012-1606(92)90161-9
DO - 10.1016/0012-1606(92)90161-9
M3 - Article
C2 - 1339336
AN - SCOPUS:0026741936
VL - 152
SP - 113
EP - 120
JO - Developmental Biology
JF - Developmental Biology
SN - 0012-1606
IS - 1
ER -