Stu2 uses a 15-nm parallel coiled coil for kinetochore localization and concomitant regulation of the mitotic spindle-Reference-Cited by-同舟云学术

Stu2 uses a 15-nm parallel coiled coil for kinetochore localization and concomitant regulation of the mitotic spindle

Published:2018-02 Issue:3 Volume:29 Page:285-294
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Haase Karen P.¹²,Fox Jaime C.¹³,Byrnes Amy E.³²,Adikes Rebecca C.⁴,Speed Sarah K.⁴,Haase Julian⁴,Friedman Brandon⁴,Cook Diana M.⁴,Bloom Kerry⁴,Rusan Nasser M.²,Slep Kevin C.⁴

Affiliation:

1. Molecular and Cellular Biophysics Program, University of North Carolina, Chapel Hill, NC 27599

2. Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892

3. Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599

4. Department of Biology, University of North Carolina, Chapel Hill, NC 27599

Abstract

The yeast microtubule polymerase Stu2’s C-terminal domain is a 15-nm parallel, homodimeric coiled coil with two spatially distinct conserved regions. Determinants in these conserved regions optimally position Stu2 on the mitotic spindle to drive proper spindle structure and dynamics.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference41 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution

2. Stu2p binds tubulin and undergoes an open-to-closed conformational change

3. Assembling the Protein Architecture of the Budding Yeast Kinetochore-Microtubule Attachment using FRET

4. A tethered delivery mechanism explains the catalytic action of a microtubule polymerase

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