Kinetics of motor protein translocation on single-stranded DNA.
The translocation of nucleic acid motor proteins along DNA or RNA can be studied in ensemble experiments by monitoring either the kinetics of the arrival of the protein at a specific site on the nucleic acid filament (generally one end of the filament) or the kinetics of ATP hydrolysis by the motor protein during translocation. The pre-steady state kinetic data collected in ensemble experiments can be analyzed by simultaneous global non-linear least squares (NLLS) analysis using a simple sequential "n-step" mechanism to obtain estimates of the rate-limiting step(s) in the translocation cycle, the average "kinetic step-size," and the efficiency of coupling ATP binding and hydrolysis to translocation.
Department of Physics and Astronomy, University of Kansas, Lawrence, KS, USA.
Christopher J
CJ
Fischer
Lake
L
Wooten
Eric J
EJ
Tomko
Timothy M
TM
Lohman
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism*; D007700:Kinetics; D008962:Models, Theoretical; D020409:Molecular Motor Proteins / Q000378:metabolism*
D004277:DNA, Single-Stranded; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases