Mutants altered in the control co-ordinating cell division with cell growth in the fission yeast Schizosaccharomyces pombe

Thuriaux, Pierre; Nurse, Paul; Carter, Bruce

doi:10.1007/bf00274190

Cited by 144 publications

(52 citation statements)

References 8 publications

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“…In contrast to swolts mutations, swo2 mutations did not cause lethality in a wee]+ background. Instead, swo2 mutants exhibited a wee phenotype at both 25 and 35°C, typical of weel-loss-of-function mutations and dominant, activating mutations of cdc2 such as cdc2-Jw and cdc2-3w (Nurse, 1975;Thuriaux et al, 1978). Genetic linkage experiments established that swo2 mutations were located at the cdc2 locus.…”

Section: Resultsmentioning

confidence: 99%

A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

1994

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Wee1 protein kinase regulates the length of G2 phase by carrying out the inhibitory tyrosyl phosphorylation of Cdc2‐cyclin B kinase. Mutations were isolated that suppressed the G2 cell cycle arrest caused by overproduction of Wee1. One class of swo (suppressor of wee1 overproduction) mutation, exemplified by swo1‐26, also caused a temperature sensitive lethal phenotype in a wee1+ background. The swo1+ gene encodes a member of the Hsp90 family of stress proteins. Swo1 is essential for viability at all temperatures. Swo1 coimmunoprecipitates with Wee1, showing that the two proteins interact. The swo1‐26 mutant undergoes premature mitosis when grown at a semi‐permissive temperature. These data strongly indicate that formation of active Wee1 tyrosine kinase requires interaction with Swo1, perhaps in a manner analogous to the previously demonstrated interaction between Hsp90 and v‐src tyrosine kinase. These observations demonstrate a unexpected role for Hsp90 in cell cycle control.

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Section: Resultsmentioning

confidence: 99%

A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

1994

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“…The transition point for the cdc2-59 cdcl3-cJ mutant was determined from cell number increase after an asynchronous culture was shifted from 25 to 36°C (Nurse et al, 1976). The medium used was PM + 0.5% yeast extract (Difco Laboratory) for the reason discussed by Thuriaux et al (1978).…”

Section: Plasmids and Yeast Transformationmentioning

confidence: 99%

Interaction between cdc13+ and cdc2+ in the control of mitosis in fission yeast; dissociation of the G1 and G2 roles of the cdc2+ protein kinase.

1987

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A cold‐sensitive (cs) allele of cdc2, a gene that acts in both the G1 and G2 phases of the fission yeast cell cycle, has been isolated by classical mutagenesis. Further mutagenesis of a cdc2cs strain yielded an extragenic suppressor that rescued the cs cell cycle defect but simultaneously conferred a temperature‐sensitive (ts) cdc phenotype. This suppressor mutation was shown to be an allele of cdc13, a previously identified gene. A variety of allele‐specific interactions between cdc2 and cdc13 were discovered. These included suppression of cdc13ts alleles by introduction of the cdc2+ gene on a multi‐copy plasmid vector. cdc13+ is required in G2 for mitotic initiation and was shown to play no role in the G1 phase of the cell cycle. cdc2+, however, is essential in G1 for DNA replication and in G2 for mitosis. The newly isolated cs allele of cdc2 that is rescued by a ts allele of cdc13 is defective only in its G2 function. cdc13+ cooperates with cdc2+ in the initiation of mitosis but not in the regulation of DNA replication. We propose that the cdc13+ gene product might be a G2‐specific substrate of the cdc2+ protein kinase.

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“…Genetic analysis indicates that the wee] + gene product (Weel) is a negative regulator of mitosis, since wee] mutant cells show a 'wee' phenotype advancing into mitosis at about half the size of wild type (Nurse, 1975;Thuriaux et al, 1978;Nurse and Thuriaux, 1980). Weel functions in opposition to Cdc25 (Fantes, 1979;Russell and Nurse, 1987b).…”

Section: Introductionmentioning

confidence: 99%

Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle.

1995

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In higher eukaryotes, the cyclin‐dependent kinases (CDKs) are negatively regulated by phosphorylation on threonine 14 (T14) and tyrosine 15 (Y15). In fission yeast, the Wee1 and mitosis inhibitory kinase 1 (Mik1) protein kinases phosphorylate Y15 in Cdc2. WEE1Hu is the only known protein kinase that can carry out this inhibitory phosphorylation on Y15 in higher eukaryotes. In the present study, we examined the endogenous products of WEE1Hu in human cells and found that the original WEE1Hu cDNA lacked 214 amino acids at the N‐terminus. The predicted full‐length protein has weak, but significant, similarity over its entire length with Mik1. Thus, we suggest that ‘WEE1Hu’ is a Mik1‐related protein rather than a Wee1 homologue. When isolated in immunoprecipitates, the endogenous WEE1Hu phosphorylated several cyclin‐associated CDKs on Y15. WEE1Hu activity increased during S and G2 phases in parallel with the level of protein. Its activity decreased at M phase when WEE1Hu became transiently hyperphosphorylated. In addition, a decrease in WEE1Hu protein level was observed at M/G1 phase. Apparently, the hyperphosphorylation and degradation in combination caused inactivation of WEE1Hu at M phase and the following G1 phase. These results suggest that the activity of WEE1Hu is regulated by phosphorylation and proteolytic degradation, and that WEE1Hu plays a role in inhibiting mitosis before M phase by phosphorylating cyclin B1‐Cdc2.

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Mutants altered in the control co-ordinating cell division with cell growth in the fission yeast Schizosaccharomyces pombe

Cited by 144 publications

References 8 publications

A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

Interaction between cdc13+ and cdc2+ in the control of mitosis in fission yeast; dissociation of the G1 and G2 roles of the cdc2+ protein kinase.

Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle.

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