Selective cleavage at lysine of the 50 kDa‐20 kDa connector loop segment of skeletal myosin S‐1 by endoproteinase Arg‐C

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Abstract
The reaction of endoproteinase Arg‐C on the skeletal myosin head heavy chain was investigated through characterization of peptides and amino acid sequence analysis. The protease splits exclusively the 50 kDa‐20 kDa junction at the lysine cluster spanning residues 639–641 and does not affect any other protease‐sensitive region of the entire myosin heavy chain. The sensitivity of the cleavage to actin and nucleotide binding makes this protease a very specific conformational probe of S‐1. The nicked S‐1 derivative, containing an intact NH2‐terminal 75 kDa fragment, may serve as a tool for gaining further insights into the domain structure and function of the myosin head.