6gx7

Publication Abstract from PubMed

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 alphaRep 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.

Insight into microtubule nucleation from tubulin-capping proteins.,Campanacci V, Urvoas A, Cantos-Fernandes S, Aumont-Nicaise M, Arteni AA, Velours C, Valerio-Lepiniec M, Dreier B, Pluckthun A, Pilon A, Pous C, Minard P, Gigant B Proc Natl Acad Sci U S A. 2019 Apr 29. pii: 1813559116. doi:, 10.1073/pnas.1813559116. PMID:31036638^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.