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Synthesis and assembly of native myosin on muscle polyribosomes
Author(s) -
Gag Jacques,
Kurowski Thomas T.,
Zak Radovan
Publication year - 1989
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(89)80794-x
Subject(s) - polysome , myosin , chemistry , biophysics , biochemistry , ribosome , biology , rna , gene
We have used the overload‐induced growth of avian muscles to study the assembly of the newly synthesized myosins which were separated by non‐denaturing pyrophosphate‐polyacrylamide gel electrophoresis. Using this model, we have observed the appearance of fast‐like isomyosins in polyribosomes prepared from slow anterior latissimus dorsi muscle after 72 h of overload. These new isoforms comigrating with native myosin from fast posterior latissimus dorsi muscle were not yet present in cellular extracts from the same muscle. The in vitro translation system utilizing muscle specific polyribosomes directs the synthesis of the corresponding myosin isoforms. Under denaturing conditions, myosin heavy chains and light chains dissociate to the expected subunit composition of each specific isoform. The synthesis and assembly of native myosin on polyribosomes indicate that myosin exists as a single mature protein prior to the incorporation in the thick filament.