Literature DB >> 17055996

Model for forward polymerization and switching transition between polymerase and exonuclease sites by DNA polymerase molecular motors.

Ping Xie1.   

Abstract

Based on the available crystal structure a model is presented for the polymerization activity and switching transition between polymerase and exonuclease sites of a DNA polymerase molecular motor. Using the model, the fast polymerization rate for correctly base-paired DNA and much reduced polymerization rate after an incorporation of a mismatched base can be well explained. The dependences of the polymerization rate and exonuclease rate on mechanical tension acting on the DNA template are studied. The switching rates between the two sites are analyzed. All the results show good quantitative agreement with the available experimental results.

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Year:  2006        PMID: 17055996     DOI: 10.1016/j.abb.2006.09.019

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  5 in total

1.  Modeling translocation dynamics of strand displacement DNA synthesis by DNA polymerase I.

Authors:  Ping Xie
Journal:  J Mol Model       Date:  2011-08-26       Impact factor: 1.810

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

Authors:  Ping Xie
Journal:  J Mol Model       Date:  2012-11-30       Impact factor: 1.810

3.  A model for transition of 5'-nuclease domain of DNA polymerase I from inert to active modes.

Authors:  Ping Xie; Jon R Sayers
Journal:  PLoS One       Date:  2011-01-14       Impact factor: 3.240

4.  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

5.  Optimal numbers of residues in linkers of DNA polymerase I, T7 primase and DNA polymerase IV.

Authors:  Yi-Ben Fu; Zhan-Feng Wang; Peng-Ye Wang; Ping Xie
Journal:  Sci Rep       Date:  2016-07-01       Impact factor: 4.379

  5 in total

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