Abstract
Brush border myosin-I (BBM-I) is a single-headed unconventional myosin found in the microvilli of intestinal epithelial cells. We used stopped-flow kinetic analysis to measure the rate and equilibrium constants for several steps in the BBM-I ATPase cycle. We determined the rates for ATP binding to BBM-I and brush border actomyosin-I (actoBBM-I), the rate of actoBBM-I dissociation by ATP, and the rates for the steps in ADP dissociation from actoBBM-I. The rate and equilibrium constants for several of the steps in the actoBBM-I ATPase are significantly different from those of other members of the myosin superfamily. Most notably, dissociation of the actoBBM-I complex by ATP and release of ADP from actoBBM-I are both very slow. The slow rates of these steps may play a role in lengthening the time spent in force-generating states and in limiting the maximal rate of BBM-I motility. In addition, release of ADP from the actoBBM-I complex occurs in at least two steps. This study provides evidence for a member of the myosin superfamily with markedly divergent kinetic behavior.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:42 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 2:25 p.m.) |
Indexed | 1 year, 5 months ago (March 18, 2024, 1:19 a.m.) |
Issued | 27 years, 8 months ago (Dec. 23, 1997) |
Published | 27 years, 8 months ago (Dec. 23, 1997) |
Published Online | 27 years, 8 months ago (Dec. 23, 1997) |
Published Print | 27 years, 8 months ago (Dec. 23, 1997) |
@article{Jontes_1997, title={Kinetic characterization of brush border myosin-I ATPase}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.26.14332}, DOI={10.1073/pnas.94.26.14332}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Jontes, James D. and Milligan, Ronald A. and Pollard, Thomas D. and Ostap, E. Michael}, year={1997}, month=dec, pages={14332–14337} }