Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities.

Nucleic Acids Research
Máté GyimesiMihály Kovács

Abstract

Quantitative determination of enzymatic rates, processivity and mechanochemical coupling is a key aspect in characterizing nucleotide triphosphate (NTP)-driven nucleic acid motor enzymes, for both basic research and technological applications. Here, we present a streamlined analytical method suitable for the determination of all key functional parameters based on measurement of NTP hydrolysis during interaction of motor enzymes with the nucleic acid track. The proposed method utilizes features of kinetic time courses of NTP hydrolysis that have not been addressed in previous analyses, and also accounts for the effect of protein traps used in kinetic experiments on processivity. This analysis is suitable for rapid and precise assessment of the effects of mutations, physical conditions, binding partners and other effectors on the functioning of translocases, helicases, polymerases and other NTP-consuming processive nucleic acid motors.

References

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Citations

Jun 6, 2012·Proceedings of the National Academy of Sciences of the United States of America·Kata SarlósMihály Kovács
Mar 10, 2010·Nucleic Acids Research·Máté GyimesiMihály Kovács
Jul 9, 2013·Biochimica Et Biophysica Acta·Erika FazekasGyöngyi Gyémánt
May 3, 2016·Methods : a Companion to Methods in Enzymology·Máté GyimesiMihály Kovács
Apr 30, 2019·International Journal of Molecular Sciences·Beata SzaboPeter Tompa
Jan 11, 2017·Proceedings of the National Academy of Sciences of the United States of America·Gábor M HaramiMihály Kovács
Jan 15, 2011·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·Ajeet K Sharma, Debashish Chowdhury

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