The role of Escherichia coli UvrB in nucleotide excision repair

Journal Article · Sat May 05 04:00:00 EDT 1990 · Journal of Biological Chemistry; (USA)

OSTI ID:6776105

Seeley, T W; Grossman, L ^[1]

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1. Johns Hopkins Univ., MD (USA)

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.

• OSTI ID: 6776105
• Journal Information: Journal of Biological Chemistry; (USA), Journal Name: Journal of Biological Chemistry; (USA) Vol. 265:13; ISSN 0021-9258; ISSN JBCHA
• Country of Publication: United States
• Language: English

Related Subjects

54 ENVIRONMENTAL SCIENCES
540130* -- Environment
Atmospheric-- Radioactive Materials Monitoring & Transport-- (1990-)
ACID ANHYDRASES
ALANINES
AMINO ACIDS
ATP-ASE
BACTERIA
BIOLOGICAL EFFECTS
BIOLOGICAL RADIATION EFFECTS
BIOLOGICAL RECOVERY
BIOLOGICAL REPAIR
CARBOXYLIC ACIDS
DNA
DNA REPAIR
ELECTROMAGNETIC RADIATION
ENZYMES
ESCHERICHIA COLI
EXCISION REPAIR
GENE MUTATIONS
GENETIC EFFECTS
GENETIC RADIATION EFFECTS
HYDROLASES
LYSINE
MICROORGANISMS
MUTATIONS
NUCLEIC ACIDS
NUCLEOPROTEINS
NUCLEOTIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHOHYDROLASES
PROTEINS
RADIATION EFFECTS
RADIATIONS
RADIOINDUCTION
RECOVERY
REPAIR
ULTRAVIOLET RADIATION