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Structural relationship between a bacterial developmental protein and eukaryotic PP2C protein phosphatases
Author(s) -
Adler Elliot,
DonellaDeana Arianna,
Arigoni Fabrizio,
Pinna Lorenzo A.,
Stragier Patrick
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.1801552.x
Subject(s) - biology , phosphatase , bacillus subtilis , kinase , phosphorylation , biochemistry , phosphoprotein , protein phosphatase 2 , transcription factor , pyruvate dehydrogenase phosphatase , saccharomyces cerevisiae , yeast , microbiology and biotechnology , genetics , enzyme , pyruvate dehydrogenase complex , gene , bacteria
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.