Isolation and structure of cat superfast myosin light chain-2 cDNA and evidence for the identity of its human homologue.
A full-length cDNA clone coding for superfast myosin light chain-2 (MyLC2) was isolated from an expression cDNA library prepared from cat masseter muscle and was fully characterized. The deduced amino acid sequence shares 58% overall identity with limb fast MyLC2, whereas homologies of the latter among higher vertebrates show 90% identity, indicating that superfast MyLC2 has diverged considerably from limb fast MyLC2 during evolution. Superfast MyLC2 cDNA has 89% nucleotide homology and 93% amino acid homology with a published novel human MyLC2 (MYL5), suggesting that MYL5 is a human homologue of the cat superfast MyLC2. Hybridization of a superfast MyLC2 isoform-specific probe reveals that expression of superfast MyLC2 in cat is confined to jaw-closing muscles. In conclusion, the present paper describes for the first time the cloning of a superfast myosin light chain coding sequence.
Qin
H
H
Department of Physiology, University of Sydney, NSW, Australia.
Morris
B J
BJ
Hoh
J F
JF
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002415:Cats; D018076:DNA, Complementary / Q000235:genetics; D005796:Genes; D006801:Humans; D008969:Molecular Sequence Data; D009218:Myosins / Q000235:genetics*; D051381:Rats; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D009218:Myosins