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Papers In Press, published online ahead of print December 23, 2005
Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405
Corresponding Author: kathleen.trybus{at}uvm.edu
Unconventional myosin V takes many 36 nm steps along an actin filament before it dissociates, thus ensuring its ability to move cargo intracellularly over long distances. Here we assess the structural features that affect processive run length by analyzing the properties of chimeras of mouse myosin V and a non-processive class V myosin from yeast (Myo4p) (Reck-Peterson et al. (2001) J. Cell Biol. 153, 1121-1126). Surprisingly, a chimera containing the yeast motor domain on the neck and rod of mouse myosin V (Y-MD) showed longer run lengths than WT at low salt. Run lengths of mouse myosin V showed little salt dependence, while those of Y-MD decreased steeply with ionic strength, similar to a chimera containing yeast loop 2 in the mouse myosin V backbone. Loop 2 binds to acidic patches on actin in the weak-binding states of the cycle (Volkmann et al. (2005) Mol. Cell 19, 595-605). Constructs containing yeast loop 2, which has no net charge compared to +6 for WT, showed a higher KM for actin in steady state ATPase assays. The results imply that a positively charged loop 2 and a high affinity for actin are important to maintain processivity near physiologic ionic strength.
J. Biol. Chem, 10.1074/jbc.M510041200
Submitted on September 13, 2005
Revised on December 5, 2005
Accepted on December 23, 2005
Processivity of chimeric class V myosins
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