PMID:2139658: Difference between revisions

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<span style = 'font-size: large'> '''Seeley, TW and Grossman, L'''  (1990) The role of Escherichia coli UvrB in nucleotide excision repair.''J. Biol. Chem.'' '''265''':7158-65</span>
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!align=left  |Citation
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'''Seeley, TW and Grossman, L'''  (1990) The role of Escherichia coli UvrB in nucleotide excision repair. ''J. Biol. Chem.'' '''265''':7158-65
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!align=left  |Abstract
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The role of UvrB in determining the nucleotide dependence of Escherichia coli excision repair has been investigated. The mutation of lysine 45 in the ATPase motif of UvrB to alanine leads to an acute defect in ATP hydrolysis and failure to support incision of UV-damaged DNA. This ATP hydrolysis activity is not required for interaction of UvrB with UvrA in solution, or for formation of a damage-independent nucleoprotein complex in the presence of UvrA and nucleotide. This UvrB mutant fails, however, to support damage-specific nucleoprotein complex formation, and does not participate in a UvrA-UvrB-dependent helicase-like activity. We conclude from these results that mutation at lysine 45 in the ATPase motif of UvrB specifically inhibits a key step in nucleotide excision repair involving the UvrB ATPase-dependent translocation of nucleoprotein complexes from undamaged to damaged DNA sites.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2139658 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || The role of UvrB in determining the nucleotide dependence of Escherichia coli excision repair has been investigated. The mutation of lysine 45 in the ATPase motif of UvrB to alanine leads to an acute defect in ATP hydrolysis and failure to support incision of UV-damaged DNA. This ATP hydrolysis activity is not required for interaction of UvrB with UvrA in solution, or for formation of a damage-independent nucleoprotein complex in the presence of UvrA and nucleotide. This UvrB mutant fails, however, to support damage-specific nucleoprotein complex formation, and does not participate in a UvrA-UvrB-dependent helicase-like activity. We conclude from these results that mutation at lysine 45 in the ATPase motif of UvrB specifically inhibits a key step in nucleotide excision repair involving the UvrB ATPase-dependent translocation of nucleoprotein complexes from undamaged to damaged DNA sites.
!align=left  |Keywords
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Adenosine Triphosphatases/metabolism; Alanine; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; DNA Damage; DNA Helicases; DNA Repair; DNA, Bacterial/radiation effects; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Lysine; Mutation; Ribonucleotides/metabolism; Ultraviolet Rays
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2139658 PubMed]
 
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==Annotations {{HelpIcon|Help:Literature}}==
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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Latest revision as of 04:38, 15 September 2013

Citation

Seeley, TW and Grossman, L (1990) The role of Escherichia coli UvrB in nucleotide excision repair. J. Biol. Chem. 265:7158-65

Abstract

The role of UvrB in determining the nucleotide dependence of Escherichia coli excision repair has been investigated. The mutation of lysine 45 in the ATPase motif of UvrB to alanine leads to an acute defect in ATP hydrolysis and failure to support incision of UV-damaged DNA. This ATP hydrolysis activity is not required for interaction of UvrB with UvrA in solution, or for formation of a damage-independent nucleoprotein complex in the presence of UvrA and nucleotide. This UvrB mutant fails, however, to support damage-specific nucleoprotein complex formation, and does not participate in a UvrA-UvrB-dependent helicase-like activity. We conclude from these results that mutation at lysine 45 in the ATPase motif of UvrB specifically inhibits a key step in nucleotide excision repair involving the UvrB ATPase-dependent translocation of nucleoprotein complexes from undamaged to damaged DNA sites.

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PubMed

Keywords

Adenosine Triphosphatases/metabolism; Alanine; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; DNA Damage; DNA Helicases; DNA Repair; DNA, Bacterial/radiation effects; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Lysine; Mutation; Ribonucleotides/metabolism; Ultraviolet Rays

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