Nucleic Acids Research, 1994, Vol. 22, No. 24 5279-5288
© 1994
Articles |
Hac1: A novel yeast bZIP protein binding to the CRE motif is a multicopy suppressor for cdcW mutant of Schizosaccharomyces pombe
Department of Molecular Genetics, Research Institute for Microbial Diseases, Osaka University 3-1 Yamadaoka, Suita, Osaka 565 1Department of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University 3-1 Yamadaoka, Suita, Osaka 565 2Mitsubishi Kasei Institute of Life Sciences 11 Minamiohya, Machida, Tokyo 194, Japan
*To whom correspondence should be addressed
+Present address: Department of Biochemistiy, Faculty of Medicine, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113, Japan
Received September 5, 1994. Accepted November 3, 1994.
We cloned by phenotypic complementation a novel Saccharomyces cerevlslae's multicopy suppressor of the Schizosaccharomyces pombe cddO-129 mutant which we call HAC1, an acronym of 'homologous to ATF/CREB 1'. It encodes a bZIP (basic-leucine zipper) protein of 230 amlno acids with close homology to the mammalian ATF/CREB transcription factor and gel-retardation assays showed that it binds specifically to the CRE motif. HAC1 is not essential for viability. However, the had disruptant becomes caffeine sensitive, which is suppressed by multicopy expression of the yeast PDE2 (Phosphodlesterase 2) gene. Although the mRNA level of HAC1 is almost constitutive throughout the cell cycle, It fluctuates during meiosis. The upstream region of the HAC1 gene contains a T4C site, a URS (upstream repression sequence) and a TR (T-rlch) box-like sequence, which reside upstream of many meiotic genes. These results suggest that HAC1 may also be one of the meiotic genes.
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