PMID:22342931: Difference between revisions
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'''Tomko, EJ, Fischer, CJ and Lohman, TM''' (2012) Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis.''J. Mol. Biol.'' '''418''':32-46 | '''Tomko, EJ, Fischer, CJ and Lohman, TM''' (2012) Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis. ''J. Mol. Biol.'' '''418''':32-46 | ||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22342931 PubMed] | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22342931 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3311787 PMC3311787] | ||
Online version:[http://dx.doi.org/10.1016/j.jmb.2012.02.013 10.1016/j.jmb.2012.02.013] | Online version:[http://dx.doi.org/10.1016/j.jmb.2012.02.013 10.1016/j.jmb.2012.02.013] | ||
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!align=left |Keywords | !align=left |Keywords | ||
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Adenosine Triphosphate/metabolism; DNA Helicases/metabolism; DNA, Single-Stranded/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Hydrolysis; Protein Transport | |||
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Latest revision as of 04:42, 15 September 2013
| Citation |
Tomko, EJ, Fischer, CJ and Lohman, TM (2012) Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis. J. Mol. Biol. 418:32-46 |
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| Abstract |
Escherichia coli UvrD is an SF1A (superfamily 1 type A) helicase/translocase that functions in several DNA repair pathways. A UvrD monomer is a rapid and processive single-stranded DNA (ssDNA) translocase but is unable to unwind DNA processively in vitro. Based on data at saturating ATP (500 μM), we proposed a nonuniform stepping mechanism in which a UvrD monomer translocates with biased (3' to 5') directionality while hydrolyzing 1 ATP per DNA base translocated, but with a kinetic step size of 4-5 nt/step, suggesting that a pause occurs every 4-5 nt translocated. To further test this mechanism, we examined UvrD translocation over a range of lower ATP concentrations (10-500 μM ATP), using transient kinetic approaches. We find a constant ATP coupling stoichiometry of ∼1 ATP/DNA base translocated even at the lowest ATP concentration examined (10 μM), indicating that ATP hydrolysis is tightly coupled to forward translocation of a UvrD monomer along ssDNA with little slippage or futile ATP hydrolysis during translocation. The translocation kinetic step size remains constant at 4-5 nt/step down to 50 μM ATP but increases to ∼7 nt/step at 10 μM ATP. These results suggest that UvrD pauses more frequently during translocation at low ATP but with little futile ATP hydrolysis. |
| Links |
PubMed PMC3311787 Online version:10.1016/j.jmb.2012.02.013 |
| Keywords |
Adenosine Triphosphate/metabolism; DNA Helicases/metabolism; DNA, Single-Stranded/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Hydrolysis; Protein Transport |
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