Structural relationship between a bacterial developmental protein and eukaryotic PP2C protein phosphatases.

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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Adler E,Donella-Deana A,Arigoni F,Pinna LA,Stragler P

doi

10.1046/j.1365-2958.1997.1801552.x

subject

Has Abstract

pub_date

1997-01-01 00:00:00

pages

57-62

issue

1

eissn

0950-382X

issn

1365-2958

journal_volume

23

pub_type

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