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An unusual catalytic subunit for the cAMP-dependent protein kinase of Dictyostelium discoideum.

Abstract：

:The cAMP-dependent protein kinase (cAPK) plays an essential role during differentiation and fruit morphogenesis in Dictyostelium discoideum. The presence of an open reading frame on the gene, pkaC (previously named either Dd PK2 or Dd PK3 by different groups), predicts a 73-kDa polypeptide with 54% similarity to the catalytic subunits of cAPKs from other organisms. Using anti-peptide antibodies, we show that the pkaC gene product, PkaC, is a 73-kDa polypeptide. Despite the fact that PkaC is about twice the size of its mammalian counterparts, it possesses all of the properties required of a catalytic subunit. It is physically associated with the regulatory subunit, and this association results in an inhibition of the catalytic activity which is reverted by cAMP. PkaC copurifies with cAPK activity, and an increased cAPK activity is observed in cells overexpressing PkaC. We conclude that PkaC is a catalytic subunit of the Dictyostelium discoideum cAPK and discuss the unusual features of this protein with the highest molecular weight of known cAPKs.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Anjard C,Etchebehere L,Pinaud S,Véron M,Reymond CD

doi

10.1021/bi00088a003

subject

Has Abstract

pub_date

1993-09-21 00:00:00

pages

9532-8

issue

37

eissn

0006-2960

issn

1520-4995

journal_volume

32

pub_type

杂志文章

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