Počet záznamů: 1
gamma-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks
- 1.
SYSNO ASEP 0489603 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název gamma-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks Tvůrce(i) Chumová, Jana (MBU-M)
Trögelová, Lucie (MBU-M) ORCID
Kourová, Hana (MBU-M)
Volc, Jindřich (MBU-M) RID
Sulimenko, Vadym (UMG-J) RID, ORCID
Halada, Petr (MBU-M) RID, ORCID
Kučera, Ondřej (URE-Y) RID
Benada, Oldřich (MBU-M) ORCID, RID
Kuchařová, A. (CZ)
Klebanovych, Anastasiya (UMG-J)
Dráber, Pavel (UMG-J) RID, ORCID
Daniel, G. (SE)
Binarová, Pavla (MBU-M) RID, ORCIDZdroj.dok. Biochimica Et Biophysica Acta-Molecular Cell Research. - : Elsevier - ISSN 0167-4889
Roč. 1865, č. 5 (2018), s. 734-748Poč.str. 15 s. Jazyk dok. eng - angličtina Země vyd. NL - Nizozemsko Klíč. slova gamma-Tubulin ; GCP-free gamma-tubulin ; Filament self-assembly Vědní obor RIV CE - Biochemie Obor OECD Microbiology Vědní obor RIV – spolupráce Ústav molekulární genetiky - Genetika a molekulární biologie CEP GA15-11657S GA ČR - Grantová agentura ČR GA16-25159S GA ČR - Grantová agentura ČR GA16-23702S GA ČR - Grantová agentura ČR LM2015062 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LO1419 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora MBU-M - RVO:61388971 ; UMG-J - RVO:68378050 ; URE-Y - RVO:67985882 UT WOS 000430031100006 EID SCOPUS 85042859952 DOI 10.1016/j.bbamcr.2018.02.009 Anotace 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2019
Počet záznamů: 1