KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry

Rogers, K.R. and Weiss, S. and Crevel, I. and Geeves, M.A. and Brophy, P.J. and Cross, R. (2001) KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry. Embo Journal, 20 (18). pp. 5101-5113. ISSN 0261-4189 . (The full text of this publication is not available from this repository)

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Abstract

The KIF1 subfamily members are monomeric and contain a number of amino acid inserts in surface loops. A particularly striking insertion of several lysine/arginine residues occurs in L12 and is called the K-loop. Two recent studies have employed both kinetic and single-molecule methods to investigate KIF1 motor properties and have produced very different conclusions about how these motors generate motility. Here we show that a hitherto unstudied member of this group, KIF1D, is not chemically processive and drives fast motility despite demonstrating a slow ATPase. The K-loop of KIF1D was analysed by deletion and insertion mutagenesis coupled with characterization by steady state and transient kinetics. Together, the results indicate that the K-loop not only increases the affinity of the motor for the MT, but crucially also inhibits its subsequent isomerization from weak to strong binding, with coupled ADP release. By stabilizing the weak binding, the K-loop establishes a pool of motors primed to undergo their power stroke.

Item Type: Article
Additional information: 0261-4189 (Print) Journal Article
Uncontrolled keywords: Adenosine Diphosphate/analogs & derivatives/metabolism Amino Acid Motifs Amino Acid Sequence Animals Anthranilic Acids/metabolism Biomechanics Kinesin/*chemistry/genetics/*physiology Kinetics Microtubules/physiology Models, Biological Molecular Motor Proteins/chemistry/genetics/physiology Molecular Sequence Data Movement Mutagenesis, Insertional Nerve Tissue Proteins/*chemistry/genetics/*physiology Protein Structure, Tertiary Sequence Deletion Sequence Homology, Amino Acid
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Michael Geeves
Date Deposited: 29 Aug 2008 14:01
Last Modified: 14 Jan 2010 14:13
Resource URI: http://kar.kent.ac.uk/id/eprint/3862 (The current URI for this page, for reference purposes)
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