Abstract
The human cardiac-actin (C H-actin) gene was transfected into rat L6 skeletal myoblasts and stable transformants were isolated. The level of the C H-actin transcript varied between clones but changed little during the differentiation of myoblasts into multinucleate myotubes. Chimeric genes were constructed in which the C H-actin promoter, first non-coding exon (44 bp), and first intron (about 700 bp) were linked to the Herpes simplex virus thymidine kinase ( tk) coding region. Clones of L6 cells transformed with these chimeric genes contained variable levels of actin- tk mRNA which changed little during differentiation. Thus, the activity of the C H-actin promoter appeared not to be up-regulated upon differentiation of myoblasts into myotubes. In clones of cells expressing the actin- tk mRNA, the TK protein was not detected in myoblasts but appeared in differentiating multinucleate myotubes. We interpret these results as suggesting developmentally regulated translation of the actin- tk mRNA. Since the first 44 nucleotides of the actin- tk mRNA were derived from the 5′-untranslated region of the C H-actin mRNA. These experiments suggest that translation of the actin- tk mRNA may be controlled by this region.
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