Difference between revisions of "Nucleotide excision repair"

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'''Nucleotide excision''' repair is a process that mends [[pyrimidine]] dimers.  In this repair pathway, an [[oligonucleotide]] containing the lesion is excised from the [[DNA]] and the resulting single-strand gap is filled in.
 
'''Nucleotide excision''' repair is a process that mends [[pyrimidine]] dimers.  In this repair pathway, an [[oligonucleotide]] containing the lesion is excised from the [[DNA]] and the resulting single-strand gap is filled in.
  
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In E. coli, pyrimidine dimers are recognized by a multisubunit enzyme, the product of the uvrA, uvrB, and uvrC genes.  This UvrABC endonuclease, is an [[ATP]]-dependent reaction, cleaves the dimer-containt DNA strand at the sevent and fourth phosphodiester bonds on the dimer's 5' and 3' sides, respectively.  The excised oligonucleotide is replaced through the action of a DNA polymerase, most probably Pol I, followed by that of DNA ligase.
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In E. coli, pyrimidine dimers are recognized by a multisubunit enzyme, the product of the uvrA, uvrB, and uvrC genes.  This UvrABC endonuclease, is an [[ATP]]-dependent reaction, cleaves the dimer-contain DNA strand at the seventh and fourth phosphodiester bonds on the dimer's 5' and 3' sides, respectively.  The excised oligonucleotide is replaced through the action of a DNA polymerase, most probably Pol I, followed by that of DNA ligase.
 
[[Category:Biochemistry]]
 
[[Category:Biochemistry]]

Revision as of 00:50, March 12, 2008

Nucleotide excision repair is a process that mends pyrimidine dimers. In this repair pathway, an oligonucleotide containing the lesion is excised from the DNA and the resulting single-strand gap is filled in.

In E. coli, pyrimidine dimers are recognized by a multisubunit enzyme, the product of the uvrA, uvrB, and uvrC genes. This UvrABC endonuclease, is an ATP-dependent reaction, cleaves the dimer-contain DNA strand at the seventh and fourth phosphodiester bonds on the dimer's 5' and 3' sides, respectively. The excised oligonucleotide is replaced through the action of a DNA polymerase, most probably Pol I, followed by that of DNA ligase.