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Stepwise modulation of ATPase activity, nucleotide trapping, and sliding motility of myosin S1 by modification of the thiol region with residues of increasing size.

MPG-Autoren
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Tiepold,  Markus
Emeritus Group Bioorganic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

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Kliche,  Werner
Emeritus Group Bioorganic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

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Pfannstiel,  Jörg
Emeritus Group Bioorganic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

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Faulstich,  Heinz
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Tiepold, M., Kliche, W., Pfannstiel, J., & Faulstich, H. (2000). Stepwise modulation of ATPase activity, nucleotide trapping, and sliding motility of myosin S1 by modification of the thiol region with residues of increasing size. Biochemistry, 39(6), 1305-1315. doi:10.1021/bi991199z.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0028-373D-2
Zusammenfassung
Rabbit muscle myosin S1 was modified either at SH1 alone or at both SH1 and SH2, using a series of alkylthiolating reagents of increasing size, designed for correlating gradually changing structural disturbances in the thiol region with functional impairments in the myosin head. The reagents were of the type H(CH(2))(n)()-S-NTB, (NTB = 2-nitro-5-thiobenzoate) (n = 1, 2, 5, 8, 9, 10, 11, and 12). Modification of only SH1 led to the expected activation of the Ca(2+)-ATPase, but only with small reagents, while reagents with n > or = 10 caused inhibition of the Ca(2+)-ATPase. Modification of both SH1 and SH2 showed the expected inhibition of Ca(2+)-ATPase but likewise allowed considerable residual Ca(2+)-ATPase activity if the residues were small. Trapping of the nucleotide, known to occur with cross-linking reagents, was seen also with monovalent reagents, provided their length exceeded n = 9 or 10. All S1 derivatives prepared in this study possessed an affinity for actin comparable to native S1 but lacked sliding motility in in vitro motility assays. The biochemical data of this study can be related to existing models of myosin S1 and recent structural data [Houdusse, A., Kalabokis, V. N., Himmel, D., Szent-Györgyi, A. G., and Cohen, C. (1999) Cell 97, 459-470] by making the assumptions that modification at SH1 prevents the formation of the SH1 helix mandatory for the transmission of conformational energy and that mobility of the thiol region is a prerequisite for ATPase activity. Immobilization of the thiol region by residues of increasing size apparently leads to lower enzyme activity and, finally, to inhibition of nucleotide exchange.