Key result
The primary structure of the heavy meromyosin region of walleye pollack myosin heavy chain was determined by cDNA cloning, revealing a sequence of 1,287 amino acids with high homology to other vertebrate myosins.
The primary structure of the heavy meromyosin region of walleye pollack myosin heavy chain was determined, providing foundational data for understanding its heat-denaturation and gel-forming properties.
Provides foundational fish myosin sequence data; leaves open any cardiac myosin homology applications pending functional studies.
Primary structure of heavy meromyosin region of walleye pollack Theragra chalcogramma myosin heavy chain was determined by cDNA cloning. By using one PCR product and five cDNA clones isolated from a λgt11-cDNA library for the pollack dorsal muscle, a nucleotide sequence of 3, 923 bp comprising 60 bp of 5'-untranslational region and 3, 863 bp of coding region was determined. The deduced sequence of 1, 287 amino acids showed considerably high homology to the corresponding regions of carp myosin (83%) and chicken and rabbit myosins (both 79%). The sequences of the regions for the putative ATP-binding, actin-binding, and regulatory light chain-binding were well conserved among the pollack, carp, chicken, and rabbit myosins (83-100% homology). On the other hand, relatively low sequence homologies were seen in the essential light chain-binding site (52-78%), junctions between 20-kDa and 50-kDa domains (27-33%) and 25-kDa and 50-kDa domains (53-57%) of subfragment-1.
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Ojima et al. (1998) studied this question. cDNA cloning was evaluated on Nucleotide and deduced amino acid sequence of the heavy meromyosin region. The primary structure of the heavy meromyosin region of walleye pollack myosin heavy chain was determined by cDNA cloning, revealing a sequence of 1,287 amino acids with high homology to other vertebrate myosins.
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