Literature DB >> 23197324

Dynamics of DNA polymerase I (Klenow fragment) under external force.

Ping Xie1.   

Abstract

During DNA synthesis, high-fidelity DNA polymerase (DNAP) translocates processively along the template by utilizing the chemical energy from nucleotide incorporation. Thus, understanding the chemomechanical coupling mechanism and the effect of external mechanical force on replication velocity are the most fundamental issues for high-fidelity DNAP. Here, based on our proposed model, we take Klenow fragment as an example to study theoretically the dynamics of high-fidelity DNAPs such as the replication velocity versus different types of external force, i.e., a stretching force on the template, a backward force on the enzyme and a forward force on the enzyme. Replication velocity as a function of the template tension with only one adjustable parameter is in good agreement with the available experimental data. The replication velocity is nearly independent of the forward force, even at very low dNTP concentration. By contrast, the backward force has a large effect on the replication velocity, especially at high dNTP concentration. A small backward force can increase the replication velocity and an optimal backward force exists at which the replication velocity has maximum value; with any further increase in the backward force the velocity decreases rapidly. These results can be tested easily by future experiments and are aid our understanding of the chemomechanical coupling mechanism and polymerization dynamics of high-fidelity DNAP.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 23197324     DOI: 10.1007/s00894-012-1688-5

Source DB:  PubMed          Journal:  J Mol Model        ISSN: 0948-5023            Impact factor:   1.810


  38 in total

1.  Temperature dependence and thermodynamics of Klenow polymerase binding to primed-template DNA.

Authors:  Kausiki Datta; Andy J Wowor; Allison J Richard; Vince J LiCata
Journal:  Biophys J       Date:  2005-12-09       Impact factor: 4.033

2.  A possible mechanism for the dynamics of transition between polymerase and exonuclease sites in a high-fidelity DNA polymerase.

Authors:  Ping Xie
Journal:  J Theor Biol       Date:  2009-04-21       Impact factor: 2.691

3.  Single molecule measurement of the "speed limit" of DNA polymerase.

Authors:  Jerrod J Schwartz; Stephen R Quake
Journal:  Proc Natl Acad Sci U S A       Date:  2009-11-11       Impact factor: 11.205

4.  Molecular motors that digest their track to rectify Brownian motion: processive movement of exonuclease enzymes.

Authors:  Ping Xie
Journal:  J Phys Condens Matter       Date:  2009-08-21       Impact factor: 2.333

5.  Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution.

Authors:  S Doublié; S Tabor; A M Long; C C Richardson; T Ellenberger
Journal:  Nature       Date:  1998-01-15       Impact factor: 49.962

6.  Structure of Taq polymerase with DNA at the polymerase active site.

Authors:  S H Eom; J Wang; T A Steitz
Journal:  Nature       Date:  1996-07-18       Impact factor: 49.962

7.  Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP.

Authors:  D L Ollis; P Brick; R Hamlin; N G Xuong; T A Steitz
Journal:  Nature       Date:  1985 Feb 28-Mar 6       Impact factor: 49.962

8.  Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance.

Authors:  H Huang; R Chopra; G L Verdine; S C Harrison
Journal:  Science       Date:  1998-11-27       Impact factor: 47.728

9.  Dependence of DNA polymerase replication rate on external forces: a model based on molecular dynamics simulations.

Authors:  Ioan Andricioaei; Anita Goel; Dudley Herschbach; Martin Karplus
Journal:  Biophys J       Date:  2004-09       Impact factor: 4.033

10.  A nucleotide binding rectification Brownian ratchet model for translocation of Y-family DNA polymerases.

Authors:  Ping Xie
Journal:  Theor Biol Med Model       Date:  2011-06-24       Impact factor: 2.432

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.