TY - JOUR
T1 - Molecular cloning of the gene for p85 that regulates the initiation of cytokinesis in Tetrahymena
AU - Gonda, Kohsuke
AU - Nishibori, Kimiko
AU - Ohba, Hiroyoshi
AU - Watanabe, Atsushi
AU - Numata, Osamu
N1 - Funding Information:
We thank Dr. Richard S. J. Weisburd for critical reading of the manuscript. We are grateful to Dr. Mariko Katoh and Dr. Izuru Yonemura for their helpful comments. This work was supported by a Research Fellowship to K. G. from the Japan Society for the Promotion of Science for Young Scientists, a Grant-in-Aid for Scientific Research to O.N. from the Ministry of Education, Sciences, Sports and Culture of Japan (06275101, 10213201), and a grant to O.N. from Yamada Science Foundation.
PY - 1999/10/14
Y1 - 1999/10/14
N2 - Tetrahymena p85 is localized to the presumptive division plane before division furrow formation; its molecular weight in SDS-polyacrylamide gel electrophoresis differs in wild-type and temperature-sensitive cell-division-arrest mutant cdaA1 cells. At the restrictive temperature, p85 localization and division furrow formation are not observed in cdaA1 cells. In this study, we purified p85 and cloned a wild-type p85 cDNA. The deduced amino acid sequence of p85 was composed mainly of two kinds of repeat sequences. One of these contained regions homologous to a calmodulin-binding site and a part of actin, and the other contained a region homologous to a part of a cdc2 kinase homologue. Moreover, we cloned a cDNA encoding the cdaA1 p85. There was no difference in the predicted amino acid sequences of wild-type and cdaA1 p85, suggesting that the difference in molecular weight between p85 in wild-type and mutant cells is caused by a disorder of posttranslational-modification mechanisms of p85 in the cdaA1 cell.
AB - Tetrahymena p85 is localized to the presumptive division plane before division furrow formation; its molecular weight in SDS-polyacrylamide gel electrophoresis differs in wild-type and temperature-sensitive cell-division-arrest mutant cdaA1 cells. At the restrictive temperature, p85 localization and division furrow formation are not observed in cdaA1 cells. In this study, we purified p85 and cloned a wild-type p85 cDNA. The deduced amino acid sequence of p85 was composed mainly of two kinds of repeat sequences. One of these contained regions homologous to a calmodulin-binding site and a part of actin, and the other contained a region homologous to a part of a cdc2 kinase homologue. Moreover, we cloned a cDNA encoding the cdaA1 p85. There was no difference in the predicted amino acid sequences of wild-type and cdaA1 p85, suggesting that the difference in molecular weight between p85 in wild-type and mutant cells is caused by a disorder of posttranslational-modification mechanisms of p85 in the cdaA1 cell.
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U2 - 10.1006/bbrc.1999.1354
DO - 10.1006/bbrc.1999.1354
M3 - Article
C2 - 10527850
AN - SCOPUS:0033554641
SN - 0006-291X
VL - 264
SP - 112
EP - 118
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -