UvrABC: Difference between revisions

Revision as of 13:17, 12 December 2016

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.
UvrB is involved in distinguishing damaged from undamaged DNA^[2].
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^[3].
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: UvrB-binding, DNA-binding and two ATP-binding domains^[4].

3D structures of UvrABC3D structures of UvrABC

Updated on 12-December-2016

ReferencesReferences

↑ 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
↑ 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

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Michal Harel, Alexander Berchansky

[1] 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

[2] 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

[3] 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

[4] 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

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@@ Line 4: / Line 4: @@
 *  '''UvrA''' is the protein which locates the DNA damage.<br />
 *  '''UvrB''' is involved in distinguishing damaged from undamaged DNA<ref>PMID:10946234</ref>.<br />
-*  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<ref>PMID:9421501</ref>.  For details on the UvrA-UvrB complex see [[UvrA-UvrB interaction domains]].
+*  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<ref>PMID:9421501</ref>.
+*  '''UvrD''' is DNA helicase II.  See [[Helicase]].
+For details on the UvrA-UvrB complex see [[UvrA-UvrB interaction domains]].
 == Structural highlights ==