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Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy
Published on: June 24, 2019
Microtubule depolymerization can drive poleward chromosome motion in fission yeast
Ekaterina L Grishchuk1, J Richard McIntosh
1MCD Biology Department, University of Colorado at Boulder, Boulder, CO 80309, USA. katya@colorado.edu
The EMBO Journal
|October 13, 2006
Summary
Poleward chromosome movements in fission yeast are not solely dependent on motor proteins. Microtubule depolymerization also drives these essential movements during cell division.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Kinetochores interact with spindle microtubules during prometaphase to ensure chromosome bi-orientation.
- Poleward movements (P-movements) of chromosomes are crucial for proper segregation and are often attributed to motor proteins.
Purpose of the Study:
- To investigate the factors driving poleward kinetochore movements in fission yeast.
- To determine the essentiality of specific motor proteins (dynein, Pkl1p, Klp2p) in mediating P-movements.
Main Methods:
- Analysis of kinetochore dynamics in fission yeast cells.
- Experimental dispersal of kinetochore-pole connections to induce recovery.
- Deletion analysis of motor protein genes (dynein, Pkl1p, Klp2p).
Main Results:
- The maximum rate of poleward kinetochore movement was not affected by the absence of any or all tested motor proteins.
- Microtubule depolymerization was identified as a significant factor contributing to P-movements in vivo.
- Klp2p, a kinetochore-localized kinesin, enhanced P-movement efficiency by promoting kinetochore fiber shortening.
Conclusions:
- Poleward kinetochore movements are not exclusively driven by known motor proteins in fission yeast.
- Microtubule dynamics, particularly depolymerization, play a critical role in chromosome movement during mitosis.
- Klp2p has a modulatory role in P-movement, distinct from its potential role as a primary driver.
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...

