The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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Authors: | ZHEN-YUAN WANG JUN SAKAI PAUL T. MATSUDAIRA IVAN C. BAINES JAMES R. SELLERS JOHN A. HAMMER III EDWARD D. KORN |
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Affiliation: | (1) Laboratory of Cell Biology, National Heart, Lung and Blood Institute, 9000 Rockville Pike, 3 Center Drive MSC 0301, Bethesda, MD 20892--0301, USA;(2) Department of Biology, Massachusetts Institute of Technology, Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142--1479, USA;(3) Laboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, 9000 Rockville Pike, 10 Center Drive MSC 1762, Bethesda, MD 20892--1762, USA |
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Abstract: | The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (50% identical) and a squidcalcium-binding protein (43% identical); the sequence is37% identical to the calcium-binding essential light chainof Physarum myosin II and 30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin |
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