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Eur J Biochem. 1984 Dec 3;145(2):221-9.

Effect of nucleotides, divalent cations and temperature on the tryptic susceptibility of myosin subfragment 1.


The kinetics of tryptic breakdown of the heavy chain of chymotryptic myosin subfragment 1 (S1) according to the following scheme (where the numbers represent approximate masses in kDa) are altered at 21 degrees C by divalent (Formula: see text) cations (Me2+) and by ATP, ADP, adenosine 5'-[beta, gamma-imino]triphosphate or PPi, with or without Me2+. ATP or its analogs slow step 2 and accelerate steps 3 and 4, while Me2+ accelerates step 2. ATP and its analogs decrease the amount of a transient 27-kDa peptide [Hozumi, T. & Muhlrad, A. (1981) Biochemistry 20, 2945-2950]. We have found direct evidence for the suggestion in this reference that the 27-kDa peptide is not an obligatory precursor of the 25-kDa fragment and that ATP or ADP suppresses the formation of the larger N-terminal fragment rather than accelerates its breakdown. Cross-linking of sulfhydryl groups located in the 20-kDa fragment leads to trapping of MgADP in the N-terminal 25-kDa peptide [Wells, J.A. & Yount, R.G. (1980) Biochemistry 19, 1711-1717]; this process affects the tryptic fragmentation of S1 similarly to, but less effectively than, nucleotides. Acts-S1 formation prevents the effect of ATP on fragmentation. At 37 degrees C S1 loses ATPase activity; tryptic digestion proceeds more rapidly and the 50-kDa and 25-kDa fragments are degraded to small peptides. Nucleotides protect against the effects of higher temperature by producing conformational changes not only in the 27-kDa N-terminal portion (containing the putative nucleotide binding site) of the heavy chain of S1 but also in the 50-kDa peptide.

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