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Vol. 16, Issue 11, 5346-5355, November 2005
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* Departments of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520-8103;
Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8103; and
Departments of Cell Biology, Yale University, New Haven, CT 06520-8103
Submitted July 6, 2005;
Revised August 19, 2005;
Accepted August 25, 2005
Monitoring Editor: Anthony Bretscher
Budding yeast possesses one myosin-II, Myo1p, whereas 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.
Abbreviations used: ELC, essential light chain; RLC, regulatory light chain; UCS, Unc-45-/Cro1p-/She4p-related.
Address correspondence to: Thomas D. Pollard (thomas.pollard{at}yale.edu).
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