• Something wrong with this record ?

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

J. Chumová, L. Trögelová, H. Kourová, J. Volc, V. Sulimenko, P. Halada, O. Kučera, O. Benada, A. Kuchařová, A. Klebanovych, P. Dráber, G. Daniel, P. Binarová,

. 2018 ; 1865 (5) : 734-748. [pub] 20180227

Language English Country Netherlands

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc18033272

γ-Tubulin is essential for microtubule nucleation and also plays less understood roles in nuclear and cell-cycle-related functions. High abundancy of γ-tubulin in acentrosomal Arabidopsis cells facilitated purification and biochemical characterization of large molecular species of γ-tubulin. TEM, fluorescence, and atomic force microscopy of purified high molecular γ-tubulin forms revealed the presence of linear filaments with a double protofilament substructure, filament bundles and aggregates. Filament formation from highly purified γ-tubulin free of γ-tubulin complex proteins (GCPs) was demonstrated for both plant and human γ-tubulin. Moreover, γ-tubulin associated with porcine brain microtubules formed oligomers. Experimental evidence on the intrinsic ability of γ-tubulin to oligomerize/polymerize was supported by conservation of α- and β-tubulin interfaces for longitudinal and lateral interactions for γ-tubulins. STED (stimulated emission depletion) microscopy of Arabidopsis cells revealed fine, short γ-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 γ-tubulin representing assemblies of higher order were localized in cell-cycle-dependent manner at sites of dispersed γ-tubulin location in acentrosomal plant cells as well as at sites of local γ-tubulin enrichment after drug treatment. Our findings that γ-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, γ-tubulin may also have scaffolding or sequestration functions.

References provided by Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc18033272
003      
CZ-PrNML
005      
20181017152643.0
007      
ta
008      
181008s2018 ne f 000 0|eng||
009      
AR
024    7_
$a 10.1016/j.bbamcr.2018.02.009 $2 doi
035    __
$a (PubMed)29499229
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a ne
100    1_
$a Chumová, Jana $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
245    10
$a γ-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks / $c J. Chumová, L. Trögelová, H. Kourová, J. Volc, V. Sulimenko, P. Halada, O. Kučera, O. Benada, A. Kuchařová, A. Klebanovych, P. Dráber, G. Daniel, P. Binarová,
520    9_
$a γ-Tubulin is essential for microtubule nucleation and also plays less understood roles in nuclear and cell-cycle-related functions. High abundancy of γ-tubulin in acentrosomal Arabidopsis cells facilitated purification and biochemical characterization of large molecular species of γ-tubulin. TEM, fluorescence, and atomic force microscopy of purified high molecular γ-tubulin forms revealed the presence of linear filaments with a double protofilament substructure, filament bundles and aggregates. Filament formation from highly purified γ-tubulin free of γ-tubulin complex proteins (GCPs) was demonstrated for both plant and human γ-tubulin. Moreover, γ-tubulin associated with porcine brain microtubules formed oligomers. Experimental evidence on the intrinsic ability of γ-tubulin to oligomerize/polymerize was supported by conservation of α- and β-tubulin interfaces for longitudinal and lateral interactions for γ-tubulins. STED (stimulated emission depletion) microscopy of Arabidopsis cells revealed fine, short γ-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 γ-tubulin representing assemblies of higher order were localized in cell-cycle-dependent manner at sites of dispersed γ-tubulin location in acentrosomal plant cells as well as at sites of local γ-tubulin enrichment after drug treatment. Our findings that γ-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, γ-tubulin may also have scaffolding or sequestration functions.
650    _2
$a mikrofilamenta $x chemie $x genetika $x ultrastruktura $7 D008841
650    _2
$a Arabidopsis $x chemie $x genetika $7 D017360
650    _2
$a cytoskelet $x chemie $x genetika $7 D003599
650    _2
$a proteiny asociované s mikrotubuly $x chemie $x genetika $7 D008869
650    _2
$a mikrotubuly $x chemie $x genetika $7 D008870
650    _2
$a mitóza $x genetika $7 D008938
650    _2
$a polymerizace $7 D058105
650    _2
$a proteinové agregáty $x genetika $7 D066329
650    _2
$a tubulin $x chemie $x genetika $x ultrastruktura $7 D014404
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Trögelová, Lucie $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Kourová, Hana $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Volc, Jindřich $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Sulimenko, Vadym $u Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Halada, Petr $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Kučera, Ondřej $u Institute of Photonics and Electronics of the Czech Academy of Sciences, Chaberská 57, 182 00 Prague 8, Czech Republic.
700    1_
$a Benada, Oldřich $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Kuchařová, Anna $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Klebanovych, Anastasiya $u Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Dráber, Pavel $u Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
700    1_
$a Daniel, Geoffrey $u Department of Forest Biomaterials Technology, Swedish University of Agricultural Sciences, Box 7008, Uppsala SE-75007, Sweden.
700    1_
$a Binarová, Pavla $u Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czech Republic. Electronic address: binarova@biomed.cas.cz.
773    0_
$w MED00000719 $t Biochimica et biophysica acta. Molecular cell research $x 0167-4889 $g Roč. 1865, č. 5 (2018), s. 734-748
856    41
$u https://pubmed.ncbi.nlm.nih.gov/29499229 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20181008 $b ABA008
991    __
$a 20181017153142 $b ABA008
999    __
$a ok $b bmc $g 1339411 $s 1030266
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2018 $b 1865 $c 5 $d 734-748 $e 20180227 $i 0167-4889 $m Biochimica et biophysica acta. Molecular cell research $n Biochem Biophys Acta $x MED00000719
LZP    __
$a Pubmed-20181008

Find record

Citation metrics

Archiving options