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Selective cleavage at lysine of the 50 kDa‐20 kDa connector loop segment of skeletal myosin S‐1 by endoproteinase Arg‐C
Author(s) -
Bertrand R.,
Derancourt J.,
Kassab R.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80277-7
Subject(s) - myosin , lysine , cleavage (geology) , chemistry , loop (graph theory) , biochemistry , biology , amino acid , paleontology , fracture (geology) , mathematics , combinatorics
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 NH 2 ‐terminal 75 kDa fragment, may serve as a tool for gaining further insights into the domain structure and function of the myosin head.