Isolation and characterization of the chicken cardiac myosin light chain (L-2A) gene. Evidence for two additional N-terminal amino acids.

The contractile proteins of striated muscle are encoded by multigene families and constitute an excellent system to investigate differentiation and developmental control of gene expression. Different forms of myosin light chains are expressed in skeletal muscle as well as in the myocard. To study the gene structure and molecular mechanisms underlying differential gene expression, the structural cardiac myosin light chain 2 (MLC-2A) gene was isolated from a chicken genomic DNA library. Restriction enzyme mapping, electron microscopic analysis, and partial sequencing revealed that the gene coding for the MLC mRNA of 700 nucleotides in length extends over 4.2 kilobases of DNA and is interrupted by 5 introns. Sequence analysis led to the detection of two codons for additional amino acids at the N terminus which were not reported to be present in the mature protein and are presumably removed post-translationally. These two amino acids, methionine and alanine, are coded on two separate exons split by the largest intron of the entire gene. Southern blot analysis of genomic chicken DNA indicates the presence of one MLC-2A gene per haploid chicken genome.