Phosphorylation of threonine residues on cloned fragments of the Dictyostelium myosin heavy chain
1988; Wiley; Volume: 227; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(88)81416-9
ISSN1873-3468
AutoresG. Wagle, Angelika A. Noegel, Jochen Scheel, Günther Gerisch,
Tópico(s)Fungal and yeast genetics research
ResumoA tail fragment of Dictyostelium discoideum myosin has been cloned and expressed as a fusion protein with the N-terminal region of MS-2 polymerase. The cloned fragment was phosphorylated with myosin heavy chain kinase II from aggregation-competent D. discoideum cells that specifically phosphorylate threonine residues on the myosin tail. Phosphopeptide maps showed the same site specificity of phosphorylation with the fusion protein as a substrate as with native myosin. An improved assay for the kinase was developed in which the fusion protein is precipitated with a monoclonal antibody that inhibits polymerization of the myosin tails without preventing their phosphorylation. Sites of phosphorylation were tentatively localized to a sequence in the C-terminal region of the heavy chain where four threonine residues are found.
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