Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F19%3A00521410" target="_blank" >RIV/86652036:_____/19:00521410 - isvavai.cz</a>

Výsledek na webu

<a href="https://science.sciencemag.org/content/363/6424/285" target="_blank" >https://science.sciencemag.org/content/363/6424/285</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1126/science.aav2567" target="_blank" >10.1126/science.aav2567</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails

Popis výsledku v původním jazyce

Microtubule doublets (MTDs), consisting of an incomplete B-microtubule at the surface of a complete A-microtubule, provide a structural scaffold mediating intraflagellar transport and ciliary beating. Despite the fundamental role of MTDs, the molecular mechanism governing their formation is unknown. We used a cell-free assay to demonstrate a crucial inhibitory role of the carboxyl-terminal (C-terminal) tail of tubulin in MTD assembly. Removal of the C-terminal tail of an assembled A-microtubule allowed for the nucleation of a B-microtubule on its surface. C-terminal tails of only one A-microtubule protofilament inhibited this side-to-surface tubulin interaction, which would be overcome in vivo with binding protein partners. The dynamics of B-microtubule nucleation and its distinctive isotropic elongation was elucidated by using live imaging. Thus, inherent interaction properties of tubulin provide a structural basis driving flagellar MTD assembly.

Název v anglickém jazyce

Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails

Popis výsledku anglicky

Microtubule doublets (MTDs), consisting of an incomplete B-microtubule at the surface of a complete A-microtubule, provide a structural scaffold mediating intraflagellar transport and ciliary beating. Despite the fundamental role of MTDs, the molecular mechanism governing their formation is unknown. We used a cell-free assay to demonstrate a crucial inhibitory role of the carboxyl-terminal (C-terminal) tail of tubulin in MTD assembly. Removal of the C-terminal tail of an assembled A-microtubule allowed for the nucleation of a B-microtubule on its surface. C-terminal tails of only one A-microtubule protofilament inhibited this side-to-surface tubulin interaction, which would be overcome in vivo with binding protein partners. The dynamics of B-microtubule nucleation and its distinctive isotropic elongation was elucidated by using live imaging. Thus, inherent interaction properties of tubulin provide a structural basis driving flagellar MTD assembly.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Science

ISSN

0036-8075

e-ISSN

—

Svazek periodika

363

Číslo periodika v rámci svazku

6424

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

4

Strana od-do

285-288

Kód UT WoS článku

000456140700037

EID výsledku v databázi Scopus

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