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. |
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. | 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. | ||
[[Category:Biochemistry]] | [[Category:Biochemistry]] | ||
Revision as of 01:06, January 13, 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-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.