C-terminal tail of tubulin mediate assembly of flagellar microtubule doublet in vitro

Date

Mar 5, 2019

Time

11:00 AM - 12:00 PM

Speaker

Marketa Cernohorska

Affiliation

Institute of Molecular Genetics of the ASCR, v. v. i., Prague, Czech Republic

Language

en

Main Topic

Biologie

Other Topics

Biologie

Host

Gaia Pigino

Description

In centriole, microtubules are assembled in conserved structure of nine-fold blades in triplets (A, B, C-microtubule) that elongates as doublets (A, B-microtubule) to the axoneme and provide scaffold for intraflagellar transport. While tough structure of these blades has long been known, the mechanism by which they form remained unknown. The most recent work on flagellar doublets using cryo-electron tomography (Ichikawa et al., 2017) suggested two possible hypotheses. First, B-microtubule is bound to A-microtubule via small microtubule inner proteins penetrating through the microtubule wall, and second, both microtubules might be bound directly via unique side-to-side contacts. In order to reveal the nature and mechanism of microtubule doublet assembly, I employed a cell-free assay combined with limited proteolytic digestion. This approach showed for the first time that microtubule doublet is assembled solely from tubulin. In this talk I will explain our discovery with Paul Guichard and Virginie Hamel of the inhibitory role of tubulin C-terminus. In addition, I will show my recent project which aims to reveal BBSome assembly using novel technique of expansion microscopy.

Last modified: Mar 6, 2019, 1:06:54 AM