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Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms
Author(s) -
Palmiter Kimberly A.,
Tyska Matthew J.,
Dupuis Donald E.,
Alpert Norman R.,
Warshaw David M.
Publication year - 1999
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1111/j.1469-7793.1999.0669n.x
Subject(s) - myosin , gene isoform , chemistry , biophysics , actin , myosin head , isometric exercise , biochemistry , myosin light chain kinase , biology , physiology , gene
1 Cardiac V3 myosin generates slower actin filament velocities and higher average isometric forces (in an in vitro motility assay) when compared with the V1 isoform. 2 To account for differences in V1 and V3 force and motion generation at the molecular level, we characterized the mechanics and kinetics of single V1 and V3 myosin molecules using a dual laser trap setup. 3 No differences in either unitary displacement (≈7 nm) or force (≈0.8 pN) were observed between isoforms; however, the duration of unitary displacement events was significantly longer for the V3 isoform at MgATP concentrations > 10 μ m . 4 Our results were interpreted on the basis of a cross‐bridge model in which displacement event durations were determined by the rates of MgADP release from, and MgATP binding to, myosin. 5 We propose that the release rate of MgADP from V3 myosin is half that of V1 myosin without any difference in their rates of MgATP binding; thus, kinetic differences between the two cardiac myosin isoforms are sufficient to account for their functional diversity.