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Journal of Experimental Biology, Vol 198, Issue 12 2501-2508, Copyright © 1995 by Company of Biologists

JOURNAL ARTICLES

Functionally significant allelic variation in myosin light chain composition in a tropical cichlid

T Crockford, I Johnston and B Mcandrew

Single fast muscle fibres in the tropical fish Oreochromis andersonii were found to contain two myosin light chains (LC1s; LC1f1* or LC1f2*). Breeding experiments confirmed that the different LC1s were of allelic origin and their inheritance patterns conformed to Mendelian expectations (1:2:1). The LC1s differed in apparent relative molecular mass by 800­900. No other differences in myosin subunits were found between the LC1 genotypes. The molar ratios of LC3:LC1(total) in the fast muscle of O. andersonii homozygous for LC1f1* or LC1f2* and heterozygous for both alleles were 2.0:1, 2.1:1 and 2.2:1, respectively, as determined by capillary electrophoresis. The maximum contraction velocity (Vmax) of single skinned muscle fibres was determined at 20 °C by the slack-test method. Vmax values (fibre lengths s-1) for fast muscle fibres from O. andersonii which were homozygous for either LC1f2* or LC1f1* were 5.3 and 3.3, respectively, compared with 3.8 when both alleles were present. Crosses between Oreochromis niloticus and O. andersonii produced F1 hybrids which were heterozygous for either LC1n/LC1f1* or LC1n/LC1f2*, where LC1n is the myosin light chain for O. niloticus. The distribution of myosin light chain genotypes in hybrid offspring was not significantly different from the expected Mendelian 1:1 ratio (47 %: 53 %). The Vmax (fibre lengths s-1) of muscle fibres containing LC1f2* from hybrid Oreochromis was 4.3 compared with 3.1 for the LC1f1* genotype. The results are consistent with a functionally significant allelic variation in myosin LC1 in fast muscle fibres from O. andersonii which is also expressed in hybrid genotypes.


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© The Company of Biologists Ltd 1995