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Conformational Studies on Activation of the E. coli uvrB Cryptic ATPase
- Source :
- Annals of the New York Academy of Sciences. 726:317-320
- Publication Year :
- 1994
- Publisher :
- Wiley, 1994.
-
Abstract
- Expression of a DNA-dependent ATPase activity by the uvrB protein is essential for early steps (preceding incision) in nucleotide excision repair (NER) in E. coli. Yet, in isolation, uvrB lacks any known catalytic ability. Its cryptic ATPase is elicited in NER by association with uvrA, but it can also be turned on by a specific, omp T-mediated proteolytic elimination of the C-terminal 43 amino acids. The truncated protein uvrB{sup *} may serve as a model for the activated structure induced by complex formation with uvrA. To probe the mechanism of activation, which may be expected to require a series of conformational changes, we have introduced the intrinsic fluorophore tryptophan (Trp) into the ATP binding site of uvrB via site-specific mutagenesis.
- Subjects :
- Protein Conformation
DNA repair
ATPase
medicine.disease_cause
General Biochemistry, Genetics and Molecular Biology
chemistry.chemical_compound
Bacterial Proteins
History and Philosophy of Science
Escherichia coli
medicine
Nucleotide
Binding site
Adenosine Triphosphatases
chemistry.chemical_classification
biology
Escherichia coli Proteins
General Neuroscience
DNA Helicases
Amino acid
Enzyme Activation
chemistry
Biochemistry
biology.protein
DNA
Nucleotide excision repair
Subjects
Details
- ISSN :
- 17496632 and 00778923
- Volume :
- 726
- Database :
- OpenAIRE
- Journal :
- Annals of the New York Academy of Sciences
- Accession number :
- edsair.doi.dedup.....0d401f48094aec9bd1935e74298cb4df