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Vol. 11, Issue 2, 523-529, February 2000
and
*Division of Molecular Medicine, Wadsworth Center, Empire State
Plaza, Albany, New York 12201-0509; and Dynein interacts with microtubules through an ATP-sensitive linkage
mapped to a structurally complex region of the heavy chain following
the fourth P-loop motif. Virtually nothing is known regarding how
binding affinity is achieved and modulated during ATP hydrolysis. We
have performed a detailed dissection of the microtubule contact site,
using fragment expression, alanine substitution, and peptide
competition. Our work identifies three clusters of amino acids
important for the physical contact with microtubules; two of these fall
within a region sharing sequence homology with MAP1B, the third in a
region just downstream. Amino acid substitutions within any one of
these regions can eliminate or weaken microtubule binding (KK3379,80,
E3385, K3387, K3397, KK3410,11, W3414, RKK3418-20, F3426, R3464,
S3466, and K3467), suggesting that their activities are highly
coordinated. A peptide that actively displaces MAP1B from microtubules
perturbs dynein binding, supporting previous evidence for similar sites
of interaction. We have also identified four amino acids whose
substitutions affect release of the motor from the microtubule (E3413,
R3444, E3460, and C3469). These suggest that nucleotide-sensitive
affinity may be locally controlled at the site of contact. Our work is
the first detailed description of dynein-tubulin interactions and
provides a framework for understanding how affinity is achieved and modulated.
Department of
Biomedical Sciences, State University of New York, Albany, New York
12201-0509
Corresponding author. E-mail
address: Michael.Koonce{at}wadsworth.org.
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