uvrD Antibody

1. Large domain movements upon UvrD dimerization and helicase activation has been reported. PMID: 29087333
2. Results show that UvrD monomer translocation rate depends on the single-stranded DNA base composition, even in the absence of any predicted basepairing within the nucleic acid. Translocation is faster on single-stranded DNA-containing pyrimidines and slower on ssDNA-containing purines PMID: 28978435
3. these data reveal that UvrD exhibits two distinct types of unwinding activity regulated by its stoichiometry. Furthermore, two UvrD conformational states, termed "closed" and "open," correlate with movement toward or away from the DNA fork. PMID: 25883359
4. The unwinding processivity is increased in the UvrD303 mutant. PMID: 24798324
5. UvrD binds RNA polymerase during transcription elongation, using its helicase/translocase activity, forces RNA polymerase to slide backward along DNA; UvrD exposes DNA lesions, allowing nucleotide excision repair enzymes to gain access to sites of damage PMID: 24402227
6. These results suggest that UvrD pauses more frequently during translocation at low ATP but with little futile ATP hydrolysis. PMID: 22342931
7. The anti-thymineless death role of UvrD. PMID: 21705756
8. crystal structure of an apo form of UvrD in which the 2B sub-domain is in an "open" state that differs by 160 degrees rotation of the 2B sub-domain PMID: 21704638
9. Although a 3'-ssDNA partial duplex provides a high-affinity site for a uvrD monomer, the study shows that a monomer also binds with specificity to DNA junctions possessing a 5'-ssDNA flanking region and can initiate translocation from this site. PMID: 20877334
10. UvrD has a critical role in the processing of DNA-protein cross-links PMID: 20444702
11. UvrD monomers translocate in discrete steps with an average kinetic step-size, m=3.68 nt step(-1), a translocation rate constant, kt=51.3 steps s(-1), with a processivity corresponding to an average translocation distance of 2400 nt before dissociation PMID: 15561144
12. mutational analysis of a thermostable UvrD helicase PMID: 15955821
13. acts by removing RecA or a RecA-made structure, allowing replication fork reversal PMID: 16135232
14. UvrD helicase is essential for Tus removal during recombination-dependent replication restart from Ter sites. PMID: 17020578
15. Role of UvrD on RecET-mediated illegitimate recombination. PMID: 17038801
16. Our results suggest that macroscopic rate of UvrD monomer translocation is not limited by each ATPase cycle but by a slow step (pause) in each translocation cycle that occurs after four to five rapid 1 nt translocation steps. PMID: 17499041
17. Results show that the anti-RecA action of UvrD at blocked forks reflects two different activities of this enzyme. PMID: 17641684
18. The multiform patterns of unwinding bursts and the distributions of the off-times favour the mechanism that UvrD unwinds DNA as a dimer. PMID: 19008855

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KEGG: ecj:JW3786

STRING: 316385.ECDH10B_4005