Resonance assignments of the microtubule-binding domain of the C-elegans spindle and kinetochore-associated protein 1

被引：4

作者：

Boeszoermenyi, Andras ^{[1
,2
]}

Schmidt, Jens C. ^{[3
,4
]}

Cheeseman, Iain M. ^{[3
,4
]}

Oberer, Monika ^{[2
]}

Wagner, Gerhard ^{[1
]}

Arthanari, Haribabu ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[2] Graz Univ, Inst Mol Biosci, A-8010 Graz, Austria

[3] MIT, Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

[4] MIT, Dept Biol, Cambridge, MA 02142 USA

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2014年 / 8卷 / 02期

基金：

奥地利科学基金会;

关键词：

Ska complex; Kinetochore; Mitosis; Microtubule; NMR resonance assignments; NMR-SPECTROSCOPY; INTERFACE; COMPLEX; SKA1; ORGANIZATION;

D O I：

10.1007/s12104-013-9499-x

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

During mitosis, kinetochores coordinate the attachment of centromeric DNA to the dynamic plus ends of microtubules, which is hypothesized to pull sister chromatids toward opposing poles of the mitotic spindle. The outer kinetochore Ndc80 complex acts synergistically with the Ska (spindle and kinetochore-associated) complex to harness the energy of depolymerizing microtubules and power chromosome movement. The Ska complex is a hexamer consisting of two copies of the proteins Ska1, Ska2 and Ska3, respectively. The C-terminal domain of the spindle and kinetochore-associated protein 1 (Ska1) is the microtubule-binding domain of the Ska complex. We solved the solution structure of the C. elegans microtubule-binding domain (MTBD) of the protein Ska1 using NMR spectroscopy. Here, we report the resonance assignments of the MTBD of C. elegans Ska1.

引用

页码：275 / 278

页数：4

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