Imperial College London

DrGeoffBaldwin

Faculty of Natural SciencesDepartment of Life Sciences

Reader in Biochemistry
 
 
 
//

Contact

 

+44 (0)20 7594 5288g.baldwin

 
 
//

Location

 

508Sir Alexander Fleming BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Bellamy:2007:nar/gkm018,
author = {Bellamy, SRW and Krusong, K and Baldwin, GS},
doi = {nar/gkm018},
journal = {Nucleic Acids Research},
pages = {1478--1487},
title = {A rapid reaction analysis of uracil DNA glycosylase indicates an active mechanism of base flipping},
url = {http://dx.doi.org/10.1093/nar/gkm018},
volume = {35},
year = {2007}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Uracil DNA glycosylase (UNG) is the primary enzymefor the removal of uracil from the genome of manyorganisms. A key question is how the enzyme isable to scan large quantities of DNA in search ofaberrant uracil residues. Central to this is themechanism by which it flips the target nucleotideout of the DNA helix and into the enzyme-active site.Both active and passive mechanisms have beenproposed. Here, we report a rapid kinetic analysisusing two fluorescent chromophores to temporallyresolve DNA binding and base-flipping with DNAsubstrates of different sequences. This studydemonstrates the importance of the protein–DNAinterface in the search process and indicates anactive mechanism by which UNG glycosylasesearches for uracil residues.
AU - Bellamy,SRW
AU - Krusong,K
AU - Baldwin,GS
DO - nar/gkm018
EP - 1487
PY - 2007///
SN - 1362-4962
SP - 1478
TI - A rapid reaction analysis of uracil DNA glycosylase indicates an active mechanism of base flipping
T2 - Nucleic Acids Research
UR - http://dx.doi.org/10.1093/nar/gkm018
UR - http://hdl.handle.net/10044/1/26427
VL - 35
ER -