A new pma1 mutation identified in a chronologically long-lived fission yeast mutant

We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1+ that encoded for an essential P-type proton ATPase. An Asp-138 to Asn mutation resulted in reduced Pma1 activity, concomitant with an increase in the chronological lifespan of this fission yeast. This study corroborates our previous report indicating Pma1 activity is crucial for the determination of life span of fission yeast, and offers information for better understanding of the enzyme, Pma1

Regulation of wee1⁺ expression during meiosis in fission yeast

<div><p>In eukaryotes, the cyclin-dependent kinase Cdk1p (Cdc2p) plays a central role in entry into and progression through nuclear division during mitosis and meiosis. Cdk1p is activated during meiotic nuclear divisions by dephosphorylation of its tyrosine-15 residue. The phosphorylation status of this residue is largely determined by the Wee1p kinase and the Cdc25p phosphatase. In fission yeast, the forkhead-type transcription factor Mei4p is essential for entry into the first meiotic nuclear division. We recently identified cdc25⁺ as an essential target of Mei4p in the control of entry into meiosis I. Here, we show that wee1⁺ is another important target of Mei4p in the control of entry into meiosis I. Mei4p bound to the upstream region of wee1⁺ in vivo and in vitro and inhibited expression of wee1⁺, whereas Mei4p positively regulated expression of the adjacent pseudogene. Overexpression of Mei4p inhibited expression of wee1⁺ and induced that of the pseudogene. Conversely, deletion of Mei4p did not decrease expression of wee1⁺ but inhibited that of the pseudogene. In addition, deletion of Mei4p-binding regions delayed repression of wee1⁺ expression as well as induction of expression of the pseudogene. These results suggest that repression of wee1⁺ expression is primarily owing to Mei4p-mediated transcriptional interference.</p></div