Article
Identification of residues within UvrB that are important for efficient DNA binding and damage processing.
The Journal of biological chemistry - 3 Dec 2004
Skorvaga Milan, DellaVecchia Matthew J, Croteau Deborah L, Theis Karsten, Truglio James J, Mandavilli Bhaskar S, Kisker Caroline, Van Houten Bennett
Abstract excerpt
The UvrB protein is the central recognition protein in bacterial nucleotide excision repair. We have shown previously that the highly conserved beta-hairpin motif in Bacillus caldotenax UvrB is essential for DNA binding, damage recognition, and UvrC-mediated incision, as deletion of the upper part of the beta-hairpin (residues 97-112) results in the inability of UvrB to be loaded onto damaged DNA, defective...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Motifs
- Bacillus
- Base Sequence
- Binding Sites
- Cholesterol
- DNA
- DNA Damage
- DNA Helicases
- DNA Repair
- Escherichia coli Proteins
- Glutamic Acid