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Functional analysis of individual brain myosin II isoforms through hybrid formation
Author(s) -
Wang Yulai,
Chantler Peter D.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00613-x
Subject(s) - gene isoform , myosin , myosin light chain kinase , immunoglobulin light chain , actin , complementary dna , biology , biochemistry , microbiology and biotechnology , gene , chemistry , genetics , antibody
We have used a scallop hybrid myosin test system in an attempt to determine the regulatory properties of an individual myosin II isoform from rat brain. The complete coding region of cDNA corresponding to a regulatory light chain isoform previously shown to be expressed in brain [Feinstein, Durand and Milner (1991) Mol. Brain Res. 10, 97‐105] was ligated within the prokaryotic expression vector, p AED4, overexpressed in bacteria, and the purified light chain incorporated within a scallop hybrid myosin. Actin activation was calcium insensitive for all hybrids tested, irrespective of whether light chain phosphorylation had taken place before, or subsequent to, hybrid formation. We discuss the implications of these results, including the possibility that these results constitute evidence for a myosin II isoform within brain that is regulated at the level of the thin filament. In addition, evidence is presented for the presence of an additional, novel isoform of regulatory light chain expressed in rat brain.