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Steady-state ATPase activity of E. coli MutS modulated by its dissociation from heteroduplex DNA
- Source :
- Biochemical and Biophysical Research Communications. 364:264-269
- Publication Year :
- 2007
- Publisher :
- Elsevier BV, 2007.
-
Abstract
- The ability of MutS to recognize mismatched DNA is required to initiate a mismatch repair (MMR) system. ATP binding and hydrolysis are essential in this process, but their role in MMR is still not fully understood. In this study, steady-state ATPase activities of MutS from Escherichia coli were investigated using the spectrophotometric method with a double end-blocked heteroduplex containing gapped bases. The ATPase activities of MutS increased as the number of gapped bases increased in a double end-blocked heteroduplex with 2-8 gapped bases in the chain, indicating that MutS dissociates from DNA when it reaches a scission during movement along the DNA. Since movement of MutS along the chain does not require extensive ATP hydrolysis and the ATPase activity is only enhanced when MutS dissociates from a heteroduplex, these results support the sliding clamp model in which ATP binding by MutS induces the formation of a hydrolysis-independent sliding clamp.
- Subjects :
- DNA, Bacterial
congenital, hereditary, and neonatal diseases and abnormalities
ATPase
Biophysics
medicine.disease_cause
Biochemistry
chemistry.chemical_compound
ATP hydrolysis
MutS-1
medicine
Molecular Biology
Escherichia coli
Adenosine Triphosphatases
DNA clamp
biology
Escherichia coli Proteins
Nucleic Acid Heteroduplexes
Cell Biology
MutS DNA Mismatch-Binding Protein
Enzyme Activation
chemistry
biology.protein
DNA mismatch repair
DNA
Heteroduplex
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 364
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....64f47500e34bcf1331ad680867fc19d7