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Reconstitution of the Very Short Patch Repair Pathway from Escherichia coli.

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Title: Reconstitution of the Very Short Patch Repair Pathway from Escherichia coli.
Authors: Robertson, Adam B.1, Matson, Steven W.1,2 smatson@bio.unc.edu
Source: Journal of Biological Chemistry. 9/21/2012, Vol. 287 Issue 39, p32953-32966. 14p.
Subjects: Escherichia coli, DNA polymerases, Proteins, Plasmids, Ligases
Abstract: The Escherichia coli very short patch (VSP) repair pathway corrects thymidine-guanine mismatches that result from spontaneous hydrolytic deamination damage of 5-methyl cytosine. The VSP repair pathway requires the Vsr endonuclease, DNA polymerase I, a DNA ligase, MutS, and MutL to function at peak efficiency. The biochemical roles of most of these proteins in the VSP repair pathway have been studied extensively. However, these proteins have not been studied together in the context of VSP repair in an in vitro system. Using purified components of the VSP repair system in a reconstitution reaction, we have begun to develop an understanding of the role played by each of these proteins in the VSP repair pathway and have gained insights into their interactions. In this report we demonstrate an in vitro reconstitution of the VSP repair pathway using a plasmid DNA substrate. Surprisingly, the repair track length can be modulated by the concentration of DNA ligase. We propose roles for MutL and MutS in coordination of this repair pathway. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Reconstitution of the Very Short Patch Repair Pathway from Escherichia coli.
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  Data: <searchLink fieldCode="AR" term="%22Robertson%2C+Adam+B%2E%22">Robertson, Adam B.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Matson%2C+Steven+W%2E%22">Matson, Steven W.</searchLink><relatesTo>1,2</relatesTo><i> smatson@bio.unc.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 9/21/2012, Vol. 287 Issue 39, p32953-32966. 14p.
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  Data: <searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22DNA+polymerases%22">DNA polymerases</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Plasmids%22">Plasmids</searchLink><br /><searchLink fieldCode="DE" term="%22Ligases%22">Ligases</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: The Escherichia coli very short patch (VSP) repair pathway corrects thymidine-guanine mismatches that result from spontaneous hydrolytic deamination damage of 5-methyl cytosine. The VSP repair pathway requires the Vsr endonuclease, DNA polymerase I, a DNA ligase, MutS, and MutL to function at peak efficiency. The biochemical roles of most of these proteins in the VSP repair pathway have been studied extensively. However, these proteins have not been studied together in the context of VSP repair in an in vitro system. Using purified components of the VSP repair system in a reconstitution reaction, we have begun to develop an understanding of the role played by each of these proteins in the VSP repair pathway and have gained insights into their interactions. In this report we demonstrate an in vitro reconstitution of the VSP repair pathway using a plasmid DNA substrate. Surprisingly, the repair track length can be modulated by the concentration of DNA ligase. We propose roles for MutL and MutS in coordination of this repair pathway. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
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  Group: Ab
  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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    Identifiers:
      – Type: doi
        Value: 10.1074/jbc.M112.384321
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      – Code: eng
        Text: English
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        PageCount: 14
        StartPage: 32953
    Subjects:
      – SubjectFull: Escherichia coli
        Type: general
      – SubjectFull: DNA polymerases
        Type: general
      – SubjectFull: Proteins
        Type: general
      – SubjectFull: Plasmids
        Type: general
      – SubjectFull: Ligases
        Type: general
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      – TitleFull: Reconstitution of the Very Short Patch Repair Pathway from Escherichia coli.
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            NameFull: Robertson, Adam B.
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              M: 09
              Text: 9/21/2012
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              Y: 2012
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              Value: 287
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              Value: 39
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