ADP release is the rate-limiting step of the MT activated ATPase of non-claret disjunctional and kinesin
- 24 July 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 368 (3) , 531-535
- https://doi.org/10.1016/0014-5793(95)00723-m
Abstract
The motor protein non-claret disjunctional (ncd) moves towards the minus ends of microtubules (MTs), whereas its close relative kinesin moves in the opposite direction towards the plus ends of MTs. The mechanisms of movement and directional reversal for these motor proteins are unknown. Here we report the rate constants for MT activated ADP release from a recombinant double-headed ncd protein, GST-MC5, and a recombinant double-headed kinesin protein, K delta 401, measured using the fluorescent nucleotide analogues methylanthranilyol ATP (mantATP) and mantADP. Comparison of the maximal MT activated mantADP release rates for these proteins with their maximal MT activated mantATP turnover rates indicates that ADP release is the rate-limiting step for ATP turnover for both ncd and kinesin. This data supports the view that directional reversal may result from structural rather than chemical kinetic differences in the way the motors interact with MTs.Keywords
This publication has 12 references indexed in Scilit:
- Pathway of processive ATP hydrolysis by kinesinNature, 1995
- Pre-Steady-State Kinetics of the Microtubule.cntdot.Kinesin ATPaseBiochemistry, 1994
- CYTOPLASMIC MICROTUBULE-ASSOCIATED MOTORSAnnual Review of Biochemistry, 1993
- Expression, purification, and characterization of the Drosophila kinesin motor domain produced in Escherichia coliBiochemistry, 1993
- Variations on the theme of movementNature, 1993
- Chemomechanical cycle of kinesin differs from that of myosinNature, 1993
- The Drosophila claret segregation protein is a minus-end directed motor moleculeNature, 1990
- Different axoplasmic proteins generate movement in opposite directions along microtubules in vitroCell, 1985
- New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as subtrates for various enzymesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- A new micromethod for the colorimetric determination of inorganic phosphateClinica Chimica Acta; International Journal of Clinical Chemistry, 1966