Function
UvrABC endonuclease is an E. coli enzyme complex involved in DNA repair. UvrABC removes 12 nucleotides around a DNA mutation replacing them with the correct one[1].
- UvrA is the protein which locates the DNA damage[2].
- UvrB is involved in distinguishing damaged from undamaged DNA[3].
- The C-terminal region of UvrC is involved in DNA binding and incisions at the 5'-side of a DNA damage during nucleotide excision repair[4].
- UvrD is DNA helicase II. See Helicase.
For details on the UvrA-UvrB complex see UvrA-UvrB interaction domains.
Structural highlights
UvrA contains several domains: [5].
3D structures of UvrABC
UvrABC 3D structures
References
- ↑ Moolenaar GF, Moorman C, Goosen N. Role of the Escherichia coli nucleotide excision repair proteins in DNA replication. J Bacteriol. 2000 Oct;182(20):5706-14. PMID:11004168
- ↑ Jaciuk M, Nowak E, Skowronek K, Tanska A, Nowotny M. Structure of UvrA nucleotide excision repair protein in complex with modified DNA. Nat Struct Mol Biol. 2011 Feb;18(2):191-7. Epub 2011 Jan 16. PMID:21240268 doi:10.1038/nsmb.1973
- ↑ Theis K, Skorvaga M, Machius M, Nakagawa N, Van Houten B, Kisker C. The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch. Mutat Res. 2000 Aug 30;460(3-4):277-300. PMID:10946234
- ↑ Moolenaar GF, Uiterkamp RS, Zwijnenburg DA, Goosen N. The C-terminal region of the Escherichia coli UvrC protein, which is homologous to the C-terminal region of the human ERCC1 protein, is involved in DNA binding and 5'-incision. Nucleic Acids Res. 1998 Jan 15;26(2):462-8. PMID:9421501
- ↑ Jaciuk M, Nowak E, Skowronek K, Tanska A, Nowotny M. Structure of UvrA nucleotide excision repair protein in complex with modified DNA. Nat Struct Mol Biol. 2011 Feb;18(2):191-7. Epub 2011 Jan 16. PMID:21240268 doi:10.1038/nsmb.1973
