Partial purification of two myosin heavy chain kinases from Dictyostelium discoideum.

Abstract:

:Myosin heavy chain kinase activity was identified in the high speed supernate of lysed Dictyostelium amoebae and was precipitated by 30-50% ammonium sulphate. In low ionic strength buffer, the activity bound tightly to a Cibacron Blue Sepharose column and eluted as a single peak with 1.0 M NaCl. Gel filtration chromatography resolved the kinase into two activities, each of which phosphorylated the tail portion of purified Dictyostelium myosin. One of these activities phosphorylated both serine and threonine residues of the heavy chain, while the other activity only phosphorylated threonine residues. Peptide mapping studies indicated that in vivo and in vitro phosphorylation sites were identical. The heavy chain kinases required Mg2+ for activity but were unaffected by Ca2+ or calmodulin. The heavy chain kinases did not phosphorylate Dictyostelium light chain, and also did not phosphorylate myosins from striated, smooth, or other nonmuscle sources.

authors

Kuczmarski ER

doi

10.1007/BF01753566

subject

Has Abstract

pub_date

1986-12-01 00:00:00

pages

501-9

issue

6

eissn

0142-4319

issn

1573-2657

journal_volume

7

pub_type

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