Arg-Pro-X-Ser/Thr is a consensus phosphoacceptor sequence for the meiosis-specific Ime2 protein kinase in Saccharomyces cerevisiae

Michael Moore, Marcus E. Shin, Adrian Bruning, Karen Schindler, Andrew Vershon, Edward Winter

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Ime2 is a meiosis-specific protein kinase in Saccharomyces cerevisiae that is functionally related to cyclin-dependent kinase. Although Ime2 regulates multiple steps in meiosis, only a few of its substrates have been identified. Here we show that Ime2 phosphorylates Sum1, a repressor of meiotic gene transcription, on Thr-306. Ime2 protein kinase assays with Sum1 mutants and synthetic peptides define a consensus Arg-Pro-X-Ser/Thr motif that is required for efficient phosphorylation by Ime2. The carboxyl residue adjacent to the phosphoacceptor (+1 position) also influences the efficiency of Ime2 phosphorylation with alanine being a preferred residue. This information has predictive value in identifying new potential Ime2 targets as shown by the ability of Ime2 to phosphorylate Sgs1 and Gip1 in vitro and could be important in differentiating mitotic and meiotic regulatory pathways.

Original languageEnglish (US)
Pages (from-to)271-278
Number of pages8
JournalBiochemistry
Volume46
Issue number1
DOIs
StatePublished - Jan 9 2007

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arginylproline
Phosphorylation
Consensus Sequence
Meiosis
Yeast
Protein Kinases
Saccharomyces cerevisiae
Cyclin-Dependent Kinases
Transcription
Alanine
Assays
Genes
Peptides
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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abstract = "Ime2 is a meiosis-specific protein kinase in Saccharomyces cerevisiae that is functionally related to cyclin-dependent kinase. Although Ime2 regulates multiple steps in meiosis, only a few of its substrates have been identified. Here we show that Ime2 phosphorylates Sum1, a repressor of meiotic gene transcription, on Thr-306. Ime2 protein kinase assays with Sum1 mutants and synthetic peptides define a consensus Arg-Pro-X-Ser/Thr motif that is required for efficient phosphorylation by Ime2. The carboxyl residue adjacent to the phosphoacceptor (+1 position) also influences the efficiency of Ime2 phosphorylation with alanine being a preferred residue. This information has predictive value in identifying new potential Ime2 targets as shown by the ability of Ime2 to phosphorylate Sgs1 and Gip1 in vitro and could be important in differentiating mitotic and meiotic regulatory pathways.",
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Arg-Pro-X-Ser/Thr is a consensus phosphoacceptor sequence for the meiosis-specific Ime2 protein kinase in Saccharomyces cerevisiae. / Moore, Michael; Shin, Marcus E.; Bruning, Adrian; Schindler, Karen; Vershon, Andrew; Winter, Edward.

In: Biochemistry, Vol. 46, No. 1, 09.01.2007, p. 271-278.

Research output: Contribution to journalArticle

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