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Titolo:
The Schizosaccharomyces pombe spo20(+) gene encoding a homologue of Saccharomyces cerevisiae Sec14 plays an important role in forespore membrane formation
Autore:
Nakase, Y; Nakamura, T; Hirata, A; Routt, SM; Skinner, HB; Bankaitis, VA; Shimoda, C;
Indirizzi:
Osaka City Univ, Grad Sch Sci, Dept Biol, Sumiyoshi Ku, Osaka 5588585, Japan Osaka City Univ Osaka Japan 5588585 , Sumiyoshi Ku, Osaka 5588585, Japan Univ Tokyo, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 1130032, Japan Univ Tokyo Tokyo Japan 1130032 r Biosci, Bunkyo Ku, Tokyo 1130032, Japan Univ Alabama, Dept Cell Biol, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Cell Biol, Birmingham, AL 35294 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 4, volume: 12, anno: 2001,
pagine: 901 - 917
SICI:
1059-1524(200104)12:4<901:TSPSGE>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHATIDYLINOSITOL-TRANSFER PROTEIN; PHOSPHOLIPASE-D ACTIVITY; CDP-CHOLINE PATHWAY; CELL-DIVISION CYCLE; SPINDLE POLE BODY; FISSION YEAST; CA2+-ACTIVATED SECRETION; ASCOSPORE FORMATION; EXPRESSION; GROWTH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Shimoda, C Osaka City Univ, Grad Sch Sci, Dept Biol, Sumiyoshi Ku, Osaka 5588585, Japan Osaka City Univ Osaka Japan 5588585 Ku, Osaka 5588585, Japan
Citazione:
Y. Nakase et al., "The Schizosaccharomyces pombe spo20(+) gene encoding a homologue of Saccharomyces cerevisiae Sec14 plays an important role in forespore membrane formation", MOL BIOL CE, 12(4), 2001, pp. 901-917

Abstract

The Schizosaccharomyces pombe spo20-KC104 mutation was originally isolatedin a screen for sporulation-deficient mutants, and the spo20-KC104 mutant exhibits temperature-sensitive growth. Herein, we report that S. pombe, spo20(+) is essential for fission yeast cell viability and is constitutively expressed throughout the life cycle. We also demonstrate that the spo20(+) gene product is structurally homologous to Saccharomyces cerevisiae Sec14, the major phosphatidylinositol transfer protein of budding yeast. This structural homology translates to a significant degree of functional relatednessbecause reciprocal complementation experiments demonstrate that each protein is able to fulfill the essential function of the other. Moreover, biochemical experiments show that, like Sec14, Spo20 is a phosphatidylinositol/phosphatidylcholine-transfer protein. That Spo20 is required for Golgi secretory function in vegetative cells is indicated by our demonstration that thespo20-KC104 mutant accumulates aberrant Golgi cisternae at restrictive temperatures. However, a second phenotype observed in Spo20-deficient fission yeast is arrest of cell division before completion of cell separation. Consistent with a direct role for Spo20 in controlling cell septation in vegetatively growing cells, localization experiments reveal that Spo20 preferentially localizes to the cell poles and to sites of septation of fission yeastcells. We also report that, when fission yeasts are challenged with nitrogen starvation, Spo20 translocates to the nucleus. This nuclear localizationpersists during conjugation and meiosis. On completion of meiosis, Spo20 translocates to forespore membranes, and it is the assembly of forespore membranes that is abnormal in spo20-KC104 cells. In such mutants, a considerable fraction of forming prespores fail to encapsulate the haploid nucleus. Our results indicate that Spo20 regulates the formation of specialized membrane structures in addition to its recognized role in regulating Golgi secretory function.

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Documento generato il 11/07/20 alle ore 18:48:48