Difference between revisions of "PMID:16829526"

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'''Croteau, DL, DellaVecchia, MJ, Wang, H, Bienstock, RJ, Melton, MA and Van Houten, B'''  (2006) The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding.''J. Biol. Chem.'' '''281''':26370-81
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!align=left  |Abstract
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In prokaryotic nucleotide excision repair, UvrA recognizes DNA perturbations and recruits UvrB for the recognition and processing steps in the reaction. One of the most remarkable aspects of UvrA is that it can recognize a wide range of DNA lesions that differ in chemistry and structure. However, how UvrA interacts with DNA is unknown. To examine the role that the UvrA C-terminal zinc finger domain plays in DNA binding, an eleven amino acid deletion was constructed (ZnG UvrA). Biochemical characterization of the ZnG UvrA protein was carried out using UvrABC DNA incision, DNA binding and ATPase assays. Although ZnG UvrA was able to bind dsDNA slightly better than wild-type UvrA, the ZnG UvrA mutant only supported 50-75% of wild type incision. Surprisingly, the ZnG UvrA mutant, while retaining its ability to bind dsDNA, did not support damage-specific binding. Furthermore, this mutant protein only provided 10% of wild-type Bca UvrA complementation for UV survival of an uvrA deletion strain. In addition, ZnG UvrA failed to stimulate the UvrB DNA damage-associated ATPase activity. Electrophoretic mobility shift analysis was used to monitor UvrB loading onto damaged DNA with wild-type UvrA or ZnG UvrA. The ZnG UvrA protein showed a 30-60% reduction in UvrB loading as compared with the amount of UvrB loaded by wild-type UvrA. These data demonstrate that the C-terminal zinc finger of UvrA is required for regulation of damage-specific DNA binding.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16829526 PubMed]
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Online version:[http://dx.doi.org/10.1074/jbc.M603093200 10.1074/jbc.M603093200]
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!align=left  |Keywords
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Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acid Sequence; DNA; DNA Damage; DNA Helicases; DNA Repair; DNA-Binding Proteins; Dimerization; Escherichia coli; Escherichia coli Proteins; Magnesium; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Fusion Proteins; Sequence Alignment; Ultraviolet Rays; Zinc Fingers
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==Main Points of the Paper ==
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{{LitSignificance}}
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== Materials and Methods Used ==
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{{LitMaterials}}
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==Phenotype Annotations==
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{|  id="M4f454b596e60e"  class=" tableEdit Phenotype_Table_2" 
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!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status
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a mutation or genetic difference within a strain
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*Taxon: Escherichia coli
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*Strain: K-12
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*Substrain:
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*NCBI Taxon ID: [http://www.ncbi.nlm.nih.gov/taxonomy?term=83333 83333]
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*Genotype of Reference Strain: ''uvrA''
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*Genotype of Experimental Strain : ''ZnG uvrA''
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*Reference Condition:
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OMP:0000303
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decreased substrate binding
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ECO:0000164
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electrophysiology assay data
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Mutant shows decreased binding affinity to damaged DNA, table 1.
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==Notes==
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==References==
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{{RefHelp}}
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<references/>
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[[Category:Publication]]

Latest revision as of 12:16, 23 February 2012

Citation

Croteau, DL, DellaVecchia, MJ, Wang, H, Bienstock, RJ, Melton, MA and Van Houten, B (2006) The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding.J. Biol. Chem. 281:26370-81

Abstract

In prokaryotic nucleotide excision repair, UvrA recognizes DNA perturbations and recruits UvrB for the recognition and processing steps in the reaction. One of the most remarkable aspects of UvrA is that it can recognize a wide range of DNA lesions that differ in chemistry and structure. However, how UvrA interacts with DNA is unknown. To examine the role that the UvrA C-terminal zinc finger domain plays in DNA binding, an eleven amino acid deletion was constructed (ZnG UvrA). Biochemical characterization of the ZnG UvrA protein was carried out using UvrABC DNA incision, DNA binding and ATPase assays. Although ZnG UvrA was able to bind dsDNA slightly better than wild-type UvrA, the ZnG UvrA mutant only supported 50-75% of wild type incision. Surprisingly, the ZnG UvrA mutant, while retaining its ability to bind dsDNA, did not support damage-specific binding. Furthermore, this mutant protein only provided 10% of wild-type Bca UvrA complementation for UV survival of an uvrA deletion strain. In addition, ZnG UvrA failed to stimulate the UvrB DNA damage-associated ATPase activity. Electrophoretic mobility shift analysis was used to monitor UvrB loading onto damaged DNA with wild-type UvrA or ZnG UvrA. The ZnG UvrA protein showed a 30-60% reduction in UvrB loading as compared with the amount of UvrB loaded by wild-type UvrA. These data demonstrate that the C-terminal zinc finger of UvrA is required for regulation of damage-specific DNA binding.

Links

PubMed Online version:10.1074/jbc.M603093200

Keywords

Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acid Sequence; DNA; DNA Damage; DNA Helicases; DNA Repair; DNA-Binding Proteins; Dimerization; Escherichia coli; Escherichia coli Proteins; Magnesium; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Fusion Proteins; Sequence Alignment; Ultraviolet Rays; Zinc Fingers

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Main Points of the Paper

Please summarize the main points of the paper.

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

See Help:AnnotationTable for details on how to edit this table.
<protect>

Phenotype of Taxon Information Genotype Information (if known) Condition Information OMP ID OMP Term Name ECO ID ECO Term Name Notes Status

a mutation or genetic difference within a strain

  • Taxon: Escherichia coli
  • Strain: K-12
  • Substrain:
  • NCBI Taxon ID: 83333
  • Genotype of Reference Strain: uvrA
  • Genotype of Experimental Strain : ZnG uvrA
  • Reference Condition:

OMP:0000303

decreased substrate binding

ECO:0000164

electrophysiology assay data

Mutant shows decreased binding affinity to damaged DNA, table 1.


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Notes

References

See Help:References for how to manage references in omp dev.

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