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• W1972056569 abstract "Molecular movements generated in the heavy-chain regions (27-50-20(× 103) Mr) of myosin S1‡ on interaction with nucleotides ATP, AMPPNP, ADP and PPi were investigated by limited proteolysis of several enzyme-metal nucleotide complexes in the absence and presence of reversibly bound and crosslinked F-actin. The rate and extent of the nucleotidepromoted conversion of the NH2-terminal 27 × 103 Mr and 50 × 103 Mr segments into products of 22 × 103 Mr and 45 × 103 Mr, respectively, were estimated to determine the amplitude of the molecular movements. The 22 × 103 Mr peptide was identified by amino acid sequence studies as being derived from cleavage of the peptide bond between Arg and Ile (at position 23 to 24). The 45 × 103 Mr, peptide, previously shown to represent the NH2-terminal part of the 50 × 103 Mr region, would be connected to the adjacent C-terminal 20 × 103 Mr region by a pre-existing loop segment of about 5 × 103 Mr; the proteolytic sensitivity of the latter region is increased particularly by nucleotide binding. The tryptic reaction proved to be a sensitive indicator of the conformational state of the liganded heavy chain as the rate of peptide bond cleavage in the two regions is dependent on the nature of the bound ligand; it decreases in the order: ATP > AMPPNP > ADP > PPi. It depends also on the nature of the metal present, Mg2+ and Ca2+ being much more effective than K+. Binding of F-actin to the S1-MgAMPPNP complex affords significant protection against breakdown of 27 × 103 Mr and 50 × 103 Mr peptides, but with concomitant hydrolysis of the 50 × 103 Mr −20 × 103 Mr junction. Additionally, interaction of MgATP with HMM modulates the tryptic fission of the S1-S2 region. The overall data provide a molecular support for the two-state model of the myosin head and emphasize the involvement of the 50 × 103 Mr unit in the mechanism of coupling between the actin and nucleotide binding sites." @default.
• W1972056569 created "2016-06-24" @default.
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• W1972056569 date "1985-06-01" @default.
• W1972056569 modified "2023-09-25" @default.
• W1972056569 title "Molecular movements promoted by metal nucleotides in the heavy-chain regions of myosin heads from skeletal muscle" @default.
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• W1972056569 doi "https://doi.org/10.1016/0022-2836(85)90015-4" @default.
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