gamma-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F18%3A00489603" target="_blank" >RIV/68378050:_____/18:00489603 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/18:00489603 RIV/67985882:_____/18:00489603

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bbamcr.2018.02.009" target="_blank" >http://dx.doi.org/10.1016/j.bbamcr.2018.02.009</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbamcr.2018.02.009" target="_blank" >10.1016/j.bbamcr.2018.02.009</a>

Jazyk výsledku

angličtina

Název v původním jazyce

gamma-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks

Popis výsledku v původním jazyce

gamma-Tubulin is essential for microtubule nucleation and also plays less understood roles in nuclear and cell-cycle-related functions. High abundancy of gamma-tubulin in acentrosomal Arabidopsis cells facilitated purification and biochemical characterization of large molecular species of gamma-tubulin. TEM, fluorescence, and atomic force microscopy of purified high molecular gamma-tubulin forms revealed the presence of linear filaments with a double protofilament substructure, filament bundles and aggregates. Filament formation from highly purified gamma-tubulin free of gamma-tubulin complex proteins (GCPs) was demonstrated for both plant and human gamma-tubulin. Moreover, gamma-tubulin associated with porcine brain microtubules formed oligomers. Experimental evidence on the intrinsic ability of gamma-tubulin to oligomerize/polymerize was supported by conservation of alpha- and beta-tubulin interfaces for longitudinal and lateral interactions for gamma-tubulins. STED (stimulated emission depletion) microscopy of Arabidopsis cells revealed fine, short gamma-tubulin fibrillar structures enriched on mitotic microtubular arrays that accumulated at polar regions of acentrosomal spindles and the outer nuclear envelope before mitosis, and were also present in nuclei. Fine fibrillar structures of gamma-tubulin representing assemblies of higher order were localized in cell-cycle-dependent manner at sites of dispersed gamma-tubulin location in acentrosomal plant cells as well as at sites of local gamma-tubulin enrichment after drug treatment. Our findings that gamma-tubulin preserves the capability of prokaryotic tubulins to self-organize into filaments assembling by lateral interaction into bundles/clusters help understanding of the relationship between structure and multiple cellular functions of this protein species and suggest that besides microtubule nucleation and organization, gamma-tubulin may also have scaffolding or sequestration functions.

Název v anglickém jazyce

gamma-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks

Popis výsledku anglicky

gamma-Tubulin is essential for microtubule nucleation and also plays less understood roles in nuclear and cell-cycle-related functions. High abundancy of gamma-tubulin in acentrosomal Arabidopsis cells facilitated purification and biochemical characterization of large molecular species of gamma-tubulin. TEM, fluorescence, and atomic force microscopy of purified high molecular gamma-tubulin forms revealed the presence of linear filaments with a double protofilament substructure, filament bundles and aggregates. Filament formation from highly purified gamma-tubulin free of gamma-tubulin complex proteins (GCPs) was demonstrated for both plant and human gamma-tubulin. Moreover, gamma-tubulin associated with porcine brain microtubules formed oligomers. Experimental evidence on the intrinsic ability of gamma-tubulin to oligomerize/polymerize was supported by conservation of alpha- and beta-tubulin interfaces for longitudinal and lateral interactions for gamma-tubulins. STED (stimulated emission depletion) microscopy of Arabidopsis cells revealed fine, short gamma-tubulin fibrillar structures enriched on mitotic microtubular arrays that accumulated at polar regions of acentrosomal spindles and the outer nuclear envelope before mitosis, and were also present in nuclei. Fine fibrillar structures of gamma-tubulin representing assemblies of higher order were localized in cell-cycle-dependent manner at sites of dispersed gamma-tubulin location in acentrosomal plant cells as well as at sites of local gamma-tubulin enrichment after drug treatment. Our findings that gamma-tubulin preserves the capability of prokaryotic tubulins to self-organize into filaments assembling by lateral interaction into bundles/clusters help understanding of the relationship between structure and multiple cellular functions of this protein species and suggest that besides microtubule nucleation and organization, gamma-tubulin may also have scaffolding or sequestration functions.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell 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

2018

Kód důvěrnosti údajů

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

Název periodika

Biochimica Et Biophysica Acta-Molecular Cell Research

ISSN

0167-4889

e-ISSN

—

Svazek periodika

1865

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

15

Strana od-do

734-748

Kód UT WoS článku

000430031100006

EID výsledku v databázi Scopus

2-s2.0-85042859952