Schizosaccharomyces pombe taf1 + is required for nitrogen starvation-induced sexual development and for entering the dormant G0 state

2001 ◽  
Vol 38 (6) ◽  
pp. 307-313 ◽  
Author(s):  
Masaru Ueno ◽  
Rumi Kurokawa ◽  
Hubert Renauld ◽  
Kousuke Watanabe ◽  
Takashi Ushimaru ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Sexual Development ◽  
Nitrogen Starvation

scholarly journals Roles of Wee1 and Nim1 protein kinases in regulating the switch from mitotic division to sexual development in Schizosaccharomyces pombe.

1997 ◽  
Vol 17 (1) ◽  
pp. 10-17 ◽  
Author(s):  
L Wu ◽  
P Russell
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Sexual Development ◽  
Cell Cycle Progression ◽  
Nitrogen Starvation ◽  
Mitotic Division ◽  
Cycle Progression ◽  
M Phase ◽  
Genes Encoding ◽  
Transcriptional Induction ◽  
Arrest Cell Cycle Progression

In self-fertile strains of the fission yeast Schizosaccharomyces pombe, nitrogen starvation initiates a program of sexual development in which cells express mating pheromones and receptors, arrest cell cycle progression in G1, and conjugate. This process is dependent on Rum1, an inhibitor of the Cdc2-Cdc13 and Cdc2-Cig2 cyclin B kinases. The M-phase induction activity of Cdc2-Cdc13 is inhibited by Wee1 tyrosine kinase, which phosphorylates Cdc2 on tyrosine-15. We report here that Wee1 activity is also important for mating. This discovery arose from studies of Nim1, a kinase which promotes mitosis by inhibiting Wee1. Nim1 was previously thought to have an important role in promoting mitosis during nitrogen starvation, but our studies revealed that Nim1 protein drops to an undetectable level within 15 min of nitrogen depletion. In contrast, Wee1 remains abundant, and tyrosine-phosphorylated Cdc2 is detected for at least 4 h after resuspension of cells in nitrogen-free medium. This suggested that maintenance of Wee1 activity may be important during the early stages of nitrogen starvation, a proposal confirmed by the observation that mating efficiency is reduced ca. fivefold in wee1- cells. Transcriptional induction of genes encoding mating factors and receptors is also delayed in wee1- cells. The wee1- mating defect is suppressed by deletion of cig2+, which encodes a B-type cyclin that promotes the onset of S and inhibits conjugation. These findings indicate that Wee1 and Rum1 act jointly to inhibit Cdc2 and promote sexual development in nitrogen-starved cells.

Analysis of the Schizosaccharomyces pombe cyclin puc1: evidence for a role in cell cycle exit

1994 ◽  
Vol 107 (3) ◽  
pp. 601-613 ◽  
Author(s):  
S.L. Forsburg ◽  
P. Nurse
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Sexual Development ◽  
Mitotic Cycle ◽  
Nitrogen Starvation ◽  
Cell Cycle Exit ◽  
Gene Encoding ◽  
Yeast Saccharomyces Cerevisiae ◽  
Protein Blocks

The puc1+ gene, encoding a G1-type cyclin from the fission yeast Schizosaccharomyces pombe, was originally isolated by complementation in the budding yeast Saccharomyces cerevisiae. Here, we report the molecular characterization of this gene and analyse its role in S. pombe. We fail to identify any function of this cyclin at the mitotic G1/S transition in S. pombe, but demonstrate that it does function in exit from the mitotic cycle. Expression of the puc1+ gene is increased during nitrogen starvation, and puc1 affects the timing of sexual development in response to starvation. Overexpression of the puc1 protein blocks sexual development, and rescues pat1ts cells, which would otherwise undergo a lethal meiosis. We conclude that puc1 contributes to negative regulation of the timing of sexual development in fission yeast, and functions at the transition between cycling and non-cycling cells.

scholarly journals Schizosaccharomyces pombe map3+ encodes the putative M-factor receptor.

1993 ◽  
Vol 13 (1) ◽  
pp. 80-88 ◽  
Author(s):  
K Tanaka ◽  
J Davey ◽  
Y Imai ◽  
M Yamamoto
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Nitrogen Starvation ◽  
Transmembrane Protein ◽  
Strong Support ◽  
Amino Acid Identity ◽  
Nucleotide Sequence Analysis ◽  
Mating Pheromone ◽  
Pheromone Signaling ◽  
P Factor ◽  
Coding Capacity

A defect in the map3 gene of the fission yeast Schizosaccharomyces pombe causes h+ mating-type-specific sterility. This gene was cloned by complementation. Nucleotide sequence analysis showed that it has a coding capacity of 365 amino acids. The deduced map3 gene product is a putative seven-transmembrane protein and has 20.0% amino acid identity with the a-factor receptor of Saccharomyces cerevisiae, encoded by STE3. It is also homologous with the Ustilago maydis mating pheromone receptors. The map3 gene is expressed in h+ cells but not in h- cells, and the transcripts are induced in response to nitrogen starvation. h+ cells defective in map3 do not respond to purified M-factor. When map3 is expressed ectopically in h- cells, they apparently acquire the ability to respond to the M-factor produced by themselves. The gpa1 gene, which encodes the alpha-subunit of a G-protein presumed to couple with the mating pheromone receptors, is essential for this function of map3. These observations strongly suggest that map3 encodes the M-factor receptor. Furthermore, this study provides strong support for the notion that pheromone signaling is essential for initiation of meiosis in S. pombe and that either M-factor signaling or P-factor signaling alone is sufficient.

Moc3, a novel Zn finger type protein involved in sexual development, ascus formation, and stress response of Schizosaccharomyces pombe

2005 ◽  
Vol 48 (6) ◽  
pp. 345-355 ◽  
Author(s):  
M Muniruzzaman Goldar ◽  
Hee Tae Jeong ◽  
Katsunori Tanaka ◽  
Hideyuki Matsuda ◽  
Makoto Kawamukai
Keyword(s):  
Stress Response ◽  
Schizosaccharomyces Pombe ◽  
Sexual Development ◽  
Type Protein

Reorganization of chromatin is an early response to nitrogen starvation in Schizosaccharomyces pombe

Chromosoma ◽  
2008 ◽  
Vol 118 (1) ◽  
pp. 99-112 ◽  
Author(s):  
Jenny Alfredsson-Timmins ◽  
Carolina Kristell ◽  
Frida Henningson ◽  
Sara Lyckman ◽  
Pernilla Bjerling
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Nitrogen Starvation ◽  
Early Response

Sexual development of Schizosaccharomyces pombe is induced by zinc or iron limitation through Ecl1 family genes

2014 ◽  
Vol 290 (1) ◽  
pp. 173-185 ◽  
Author(s):  
Hokuto Ohtsuka ◽  
Maiko Ishida ◽  
Chikako Naito ◽  
Hiroshi Murakami ◽  
Hirofumi Aiba
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Sexual Development ◽  
Iron Limitation

scholarly journals Cig2, a B-type cyclin, promotes the onset of S in Schizosaccharomyces pombe.

1996 ◽  
Vol 16 (4) ◽  
pp. 1527-1533 ◽  
Author(s):  
O Mondesert ◽  
C H McGowan ◽  
P Russell
Keyword(s):  
Dna Replication ◽  
Schizosaccharomyces Pombe ◽  
Double Mutant ◽  
Kinase Activity ◽  
Nitrogen Starvation ◽  
Gradual Increase ◽  
S Phase ◽  
G1 Arrest ◽  
Cyclin Dependent Kinases ◽  
M Phase

Cdc2, a catalytic subunit of cyclin-dependent kinases, is required for both the G1-to-S and G2-to-M transitions in the fission yeast Schizosaccharomyces pombe. Cdc13, a B-type cyclin, is required for the M-phase induction function of Cd2. Two additional B-type cyclins, Cig1 and Cig2, have been identified in S. pombe, but none of the B-type cyclins are individually required for the onset of S. We report that Cdc13 is important for DNA replication in a strain lacking Cig2. Unlike deltacdc13 cells, double-mutant deltacdc13 deltacig2 cells are defective in undergoing multiple rounds of DNA replication. The conclusion that Cig2 promotes S is further supported by the finding that Cig2 protein and Cig2-associated kinase activity appear soon after the completion of M and peak during S, as well as the observation that S is delayed in deltacig2 cells as they recover from a G1 arrest induced by nitrogen starvation. These studies indicate that Cig2 is the primary S-phase-promoting cyclin in S. pombe but that Cdc13 can effectively substitute for Cig2 in deltacig2 cells. These observations also suggest that the gradual increase in the activity of Cdc2-Cdc13 kinase can be sufficient for the correct temporal ordering of S and M phases in deltacig2 cells.

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