Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 116, Issue 20, Pages 9859-9864Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1813559116
Keywords
cytoskeleton; microtubule nucleation; structural biology; CopN; artificial binding proteins
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Funding
- ARC Foundation for Cancer Research
- CNRS and INSERM
- French National Research Agency [ANR-17-CE09-0040]
- French Infrastructure for Integrated Structural Biology [ANR-10-INSB-05-01]
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Nucleation is one of the least understood steps of microtubule dynamics. It is a kinetically unfavorable process that is templated in the cell by the gamma-tubulin ring complex or by preexisting microtubules; it also occurs in vitro from pure tubulin. Here we study the nucleation inhibition potency of natural or artificial proteins in connection with their binding mode to the longitudinal surface of alpha- or beta-tubulin. The structure of tubulin-bound CopN, a Chlamydia protein that delays nucleation, suggests that this protein may interfere with two protofilaments at the (+) end of a nucleus. Designed ankyrin repeat proteins that share a binding mode similar to that of CopN also impede nucleation, whereas those that target only one protofilament do not. In addition, an alpha Rep protein predicted to target two protofilaments at the (-) end does not delay nucleation, pointing to different behaviors at both ends of the nucleus. Our results link the interference with protofilaments at the (+) end and the inhibition of nucleation.
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