PROTEIN-KINASE ACTIVITY ASSOCIATED WITH THE IME2 GENE-PRODUCT, A MEIOTIC INDUCER IN THE YEAST SACCHAROMYCES-CEREVISIAE

被引:34
作者
KOMINAMI, K [1 ]
SAKATA, Y [1 ]
SAKAI, M [1 ]
YAMASHITA, I [1 ]
机构
[1] HIROSHIMA UNIV, CTR GENE SCI, HIROSHIMA 724, JAPAN
关键词
D O I
10.1271/bbb.57.1731
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The IME2 gene product (Ime2) is required for entry into meiosis and sporulation in S. cerevisiae. It has been predicted to be composed of two domains, an amino-terminal domain with homology to protein kinases and a carboxy-terminal acidic domain. The Ime2 was identified in extracts of meiotic cells carrying multi- but not low-copy IME2 in immunoblot analysis using an Ime2-specific antibody. Immune complexes were found to phosphorylate Ime2 and several exogenous proteins. Low-copy plasmids expressing truncated Ime2 proteins that lack part of or the entire carboxy-terminal domain enabled cells to undergo sporulation even under a certain repressive nutritional condition. These cells contained increased levels of protein kinase activity compared with control cells. These results suggest that the amino-terminal domain has a protein kinase activity and that the acidic tail is not essential for either the kinase activity or sporulation but serves in a negative role. An Ime2-beta-galactosidase fusion was shown by immunofluorescence microscopy to be localized predominantly to the nucleus, suggesting a nuclear function of Ime2.
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页码:1731 / 1735
页数:5
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