期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：11
页码：4467-4471
DOI：10.1073/pnas.71.11.4467
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Cytoplasmic polyadenylylated messenger RNA from differentiated muscle cultures, when incubated in a wheat germ cell-free system, directed the synthesis of a polypeptide indistinguishable from authentic chicken skeletal muscle actin, as judged by mobility on sodium dodecyl sulfate-polyacrylamide gels, tryptic peptide analyses, and biological activity. The synthesis of actin in the cell-free system was used to assay levels of translatable actin mRNA in cultures of fibroblasts, pre- and post-fusion myoblasts, and myoblasts grown under conditions that prevent fusion. In all cases the amount of actin polypeptide synthesized in the cell-free system was proportional to the rate of actin synthesis in the cultures from which the RNA was extracted. It is suggested that actin synthesis is regulated by the actin mRNA content of the cell and that an increase in the cytoplasmic level of translatable actin messenger RNA is mediated by cell fusion rather than by the terminal round of DNA synthesis.
