MG_073_206_421_TETRAMER – DNA incision complex

WID MG_073_206_421_TETRAMER View in model
Name DNA incision complex View in model
Cross references PDB: 1QOJ
Biosynthesis [c]: MG_073_MONOMER + MG_206_MONOMER + (2) MG_421_MONOMERMG_073_206_421_TETRAMER View in model
No. subunits 4
DNA footprint Length: 18 (nt), Binding: dsDNA, Region: dsDNA View in model
Empirical formula (pH 7.5) H25834C16022N4327O4717S76
Molecular weight (pH 7.5; Da) 356986.62 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200.00 View in model
Formation process Process_MacromolecularComplexation View in model
Localization c
Enzyme DNA incision
[c]: ATP + (2) dRibose5P_dRibose5P + (3) H2OADP + (4) DR5P + (3) H + PI
View in model
Reaction participant View in model
Complex subunit DNA incision complex
[c]: MG_073_MONOMER + MG_206_MONOMER + (2) MG_421_MONOMERMG_073_206_421_TETRAMER
View in model
Parameters View in model
Comments UvrA, UvrB, and UvrC form complexes that recognize DNA damage, and incise DNA 3' and 5' to damaged lesions in nucleotide excision repair. UvrA-C function according to the scheme below [PUB_0461]: UvrA2B complex recognizes DNA damage UvrA hydrolyzes ATP and dissociates from UvrB, leaving a DNA-UvrB complex UvrC complexes with UvrB, inducing a conformational change in UvrB which nicks the DNA 4 nt 3' to the damage UvrC nicks the DNA 7 nt 5' to the damage DNA-binding Distances between 3' and 5' cleavages is 12 bp [PUB_0461]. UvrAB footprint is 10 nt [PUB_0713], 18 nt [PUB_0709], 19 nt [PUB_0710], 20 nt [PUB_0712]. UvrA2 and UvrB have footprints of 33 nt and 24 nt [PUB_0515]. Composition [PUB_0006].
  1. Friedberg EC, Walker GC, Siede W, Wood RD, Schultz RA, Ellenberger T. DNA repair and mutagenesis. ASM Press (2006). WholeCell: PUB_0461, ISBN: 9781555813192

  2. Keseler IM, Bonavides-Martínez C, Collado-Vides J, Gama-Castro S, Gunsalus RP, Johnson DA, Krummenacker M, Nolan LM, Paley S, Paulsen IT, Peralta-Gil M, Santos-Zavaleta A, Shearer AG, Karp PD. EcoCyc: a comprehensive view of Escherichia coli biology. Nucleic Acids Res 37, D464-70 (2009). WholeCell: PUB_0006, PubMed: 18974181

  3. Minko IG, Zou Y, Lloyd RS. Incision of DNA-protein crosslinks by UvrABC nuclease suggests a potential repair pathway involving nucleotide excision repair. Proc Natl Acad Sci U S A 99, 1905-9 (2002). WholeCell: PUB_0713, PubMed: 11842222

  4. Seeberg E, Fuchs RP. Acetylaminofluorene bound to different guanines of the sequence -GGCGCC- is excised with different efficiencies by the UvrABC excision nuclease in a pattern not correlated to the potency of mutation induction. Proc Natl Acad Sci U S A 87, 191-4 (1990). WholeCell: PUB_0709, PubMed: 2296578

  5. Van Houten B, Gamper H, Sancar A, Hearst JE. DNase I footprint of ABC excinuclease. J Biol Chem 262, 13180-7 (1987). WholeCell: PUB_0710, PubMed: 3308871

  6. ... 2 more

  7. Visse R, de Ruijter M, Moolenaar GF, van de Putte P. Analysis of UvrABC endonuclease reaction intermediates on cisplatin-damaged DNA using mobility shift gel electrophoresis. J Biol Chem 267, 6736-42 (1992). WholeCell: PUB_0712, PubMed: 1551881

  8. Zou Y, Liu TM, Geacintov NE, Van Houten B. Interaction of the UvrABC nuclease system with a DNA duplex containing a single stereoisomer of dG-(+)- or dG-(-)-anti-BPDE. Biochemistry 34, 13582-93 (1995). WholeCell: PUB_0515, PubMed: 7577947

Created 2012-10-01 15:07:37
Last updated 2012-10-01 15:14:04