Synthesis and assembly of native myosin on muscle polyribosomes

FEBS Letters

Zak, Radovan¹  Gagnon, Jacques¹  Kurowski, Thomas T.¹ 

[1] Department of Medicine and Pharmacological and Physiological Sciences, The University of Chicago, 5841 South Maryland Ave, Chicago, IL 60637, USA

关键词: Myosin isoform;    Myosin heavy chain;    Myosin light chain;    Overload hypertrophy;    (Chicken skeletal muscle);    ALD;    anterior latissimus dorsi muscle;    PLD;    posterior latissimus dorsi muscle;    SM1;    SM2;    slow isomyosin 1;    slow isomyosin 2;    FM1;    FM2;    FM3;    fast isomyosin 1;    fast isomyosin 2;    fast isomyosin 3;    MHC;    myosin heavy chain;    MLC;    myosin light chain;    PP-PAGE;    non-denaturing pyrophosphate-polyacrylamide gel electrophoresis;    SDS-PAGE;    denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(89)80794-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown