LOCALIZATION OF THE NOVEL RNA BINDING PROTEIN SLA1 AND ITS ROLE IN CELL DIFFERENTIATION IN FISSION YEAST
| Project/Area Number |
12660301
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | SHIMANE UNIVERSITY |
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Principal Investigator |
KAWAMUKAI Makoto SHIMANE UNIVERSITY, LIFE AND ENVIRONMENTAL SCIENCE, PROFESSOR, 生物資源科学部, 教授 (70186138)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2001: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2000: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | RAS / cAMP / Signal transduction / fission yeast / Sla1 / Sla1 |
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| Research Abstract |
Sla1, a homolog of human La protein in fission yeast, has been known to be an RNA binding protein that has an RRM (RNA-Recognition Motif) and the La motif which are highly conserved among La protein families. In this study, we present the evidence, for the first time among the La homologs, that a truncated form of Sla1 is important for regulation of sexual development in Schizosaccharomyces pombe. We found that Sla1 truncated in the COOH-terminus (Sla1DC) induced ectopic sporulation in ras1 strain and other several sporulation deficient strains such as disruptants of the components of the MAPK-cascade, the SAPK-cascade and the cAMP-cascade. The full-length of Sla1 located in nucleus, but sporulation inducible Sla1DC located in cytoplasm. Consistent with this result, Sla1 has a basic NLS (Nuclear Localization Signal)-like motif in its COOH terminus. Further deletion analysis of Sla1 suggested that for sporulation inducible effect a small region that includes only a portion of RRM, but neither a whole RRM nor the La motif was required. In addition, Sla1DC induced ectopic haploid meiosis, like pat1-114 or mei2-SATA mutant do. Sla1DC induced sporulation in a mei3 disruptant but not in a mei2 disruptant. These results strongly suggested that Sla1DC acts at the upstream of Mei2 and at the downstream of Mei3.
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Report
(3 results)
Research Products
(12 results)
