ArticleDNA repair2008
Cooperative damage recognition by UvrA and UvrB: identification of UvrA residues that mediate DNA binding.
Article in DNA repair, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Persistent effects of early-life arsenic exposure inEnvironmental science. Processes & impacts · 2026Article
- Advances in stress-tolerance elements for microbial cell factories.Synthetic and systems biotechnology · 2024Review
- Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER.Nucleic acids research · 2023Article
- Single-molecule imaging reveals molecular coupling between transcription and DNA repair machinery in live cells.Nature communications · 2020Article
- The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.Nucleic acids research · 2019Article
- Article
- Spore photoproduct within DNA is a surprisingly poor substrate for its designated repair enzyme-The spore photoproduct lyase.DNA repair · 2017Article
- Single-Molecule Methods for Nucleotide Excision Repair: Building a System to Watch Repair in Real Time.Methods in enzymology · 2017Article
- Effects of reduced mitochondrial DNA content on secondary mitochondrial toxicant exposure in Caenorhabditis elegans.Mitochondrion · 2016Article
- Spore photoproduct lyase: the known, the controversial, and the unknown.The Journal of biological chemistry · 2015Review
- Ribonucleotides as nucleotide excision repair substrates.DNA repair · 2014Article
- Removal of misincorporated ribonucleotides from prokaryotic genomes: an unexpected role for nucleotide excision repair.PLoS genetics · 2013Article
- Prokaryotic nucleotide excision repair.Cold Spring Harbor perspectives in biology · 2013Review
- Article
- Dynamics of lesion processing by bacterial nucleotide excision repair proteins.Progress in molecular biology and translational science · 2012Review
- The biological and structural characterization of Mycobacterium tuberculosis UvrA provides novel insights into its mechanism of action.Nucleic acids research · 2011Article
- Hpy188I-DNA pre- and post-cleavage complexes--snapshots of the GIY-YIG nuclease mediated catalysis.Nucleic acids research · 2011Article
- Structure of UvrA nucleotide excision repair protein in complex with modified DNA.Nature structural & molecular biology · 2011Article
- DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Nucleotide excision repair (NER) is responsible for the recognition and removal of numerous structurally unrelated DNA lesions. In prokaryotes, the proteins UvrA, UvrB and UvrC orchestrate the recognition and excision of aberrant lesions from DNA. Despite the progress we have made in understanding the NER pathway, it remains unclear how the UvrA dimer interacts with DNA to facilitate DNA damage recognition. The purpose of this study was to define amino acid residues in UvrA that provide binding energy to DNA. Based on conservation among approximately 300 UvrA sequences and 3D-modeling, two positively charged residues, Lys680 and Arg691, were predicted to be important for DNA binding. Mutagenesis and biochemical analysis of Bacillus caldontenax UvrA variant proteins containing site directed mutations at these residues demonstrate that Lys680 and Arg691 make a significant contribution toward the DNA binding affinity of UvrA. Replacing these side chains with alanine or negatively charged residues decreased UvrA binding 3-37-fold. Survival studies indicated that these mutant proteins complemented a WP2 uvrA(-) strain of bacteria 10-100% of WT UvrA levels. Further analysis by DNase I footprinting of the double UvrA mutant revealed that the UvrA DNA binding defects caused a slower rate of transfer of DNA to UvrB. Consequently, the mutants initiated the oligonucleotide incision assay nearly as well as WT UvrA thus explaining the observed mild phenotype in the survival assay. Based on our findings we propose a model of how UvrA binds to DNA.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.