Abstract
Bacillus subtilis SpoIIE is a Ser protein phosphatase whose action on the phosphoprotein SpoIIAA triggers the cell type-specific activation of a sporulation transcription factor. Here we report that SpoIIE displays sequence similarity to the PP2C family of eukaryotic Ser/Thr protein phosphatases, and that residues common to these proteins are required for the function of both SpoIIE and TPD1, a yeast PP2C. These findings suggest that SpoIIE and the PP2C protein phosphatases are structurally related, and reveal a striking formal similarity between the SpoIIAA regulatory circuit and that of mammalian mitochondrial pyruvate dehydrogenase. This similarity may reflect an evolutionarily conserved mechanism of biological regulation based on the interplay of His protein kinase-like Ser kinases and PP2C-like protein phosphatases.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Aspartic Acid*
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Bacillus subtilis / enzymology*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Eukaryotic Cells
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Humans
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Phosphoprotein Phosphatases / chemistry*
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Phosphoprotein Phosphatases / genetics
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Phosphoprotein Phosphatases / metabolism
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Protein Phosphatase 2
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Protein Phosphatase 2C
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Saccharomyces cerevisiae Proteins*
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Sigma Factor*
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Structure-Activity Relationship
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Transcription Factors*
Substances
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Bacterial Proteins
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Fungal Proteins
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Saccharomyces cerevisiae Proteins
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Sigma Factor
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Transcription Factors
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spoIIR protein, Bacillus subtilis
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spore-specific proteins, Bacillus
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Aspartic Acid
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PTC1 protein, S cerevisiae
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Phosphoprotein Phosphatases
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Protein Phosphatase 2
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Protein Phosphatase 2C