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MBC in Press, published online ahead of print September 7, 2005
Mol. Biol. Cell 10.1091/mbc.E05-07-0601

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Submitted on July 6, 2005
Revised on August 19, 2005
Accepted on August 25, 2005

Cytokinesis Depends on the Motor Domains of Myosin-II in Fission Yeast but Not in Budding Yeast

Matthew Lord,* Ellen Laves,* and Thomas D. Pollard{dagger}{ddagger}

Departments of *Molecular, Cellular, and Developmental Biology, {dagger}Molecular Biophysics & Biochemistry, and {ddagger}Cell Biology, Yale University, New Haven, CT 06520-8103

Monitoring Editor: Anthony Bretscher

Budding yeast possesses one myosin-II, Myo1p, while fission yeast has two, Myo2p and Myp2p, all of which contribute to cytokinesis. We find that chimeras consisting of Myo2p or Myp2p motor domains fused to the tail of Myo1p are fully functional in supporting budding yeast cytokinesis. Remarkably, the tail alone of budding yeast Myo1p localizes to the contractile ring supporting both its constriction and cytokinesis. In contrast, fission yeast Myo2p and Myp2p require both the catalytic head domain as well as tail domains for function, with the tails providing distinct functions (Bezanilla and Pollard, 2000). Myo1p is the first example of a myosin whose cellular function does not require a catalytic motor domain revealing a novel mechanism of action for budding yeast myosin-II independent of actin-binding and ATPase activity.

Address correspondence to: Thomas D. Pollard (thomas.pollard{at}yale.edu)




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