Non-replicative helicases at the replication fork Journal Article
| Authors: | Heller, R. C.; Marians, K. J. |
| Article Title: | Non-replicative helicases at the replication fork |
| Abstract: | Reactivation of stalled or collapsed replication forks is an essential process in bacteria. Restart systems operate to restore the 5′ → 3′ replicative helicase, DnaB, to the lagging-strand template. However, other non-replicative 3′ → 5′ helicases play an important role in the restart process as well. Here we examine the DNA-binding specificity of three of the latter group, PriA, Rep, and UvrD. Only PriA and Rep display structure-specific fork binding. Interestingly, their specificity is opposite: PriA binds a leading-strand fork, presumably reflecting its restart activity in directing loading of DnaB to the lagging-strand template. Rep binds a lagging-strand fork, presumably reflecting its role in partially displacing Okazaki fragments that originate near the fork junction. This activity is necessary for generating a single-stranded landing pad for DnaB. While UvrD shows little structure-specificity, there is a slight preference for lagging-strand forks, suggesting that there might be some redundancy between Rep and UvrD and possibly explaining the observed synthetic lethality that occurs when mutations in the genes encoding these two proteins are combined. © 2007 Elsevier B.V. All rights reserved. |
| Keywords: | unclassified drug; gene mutation; dna-binding proteins; nonhuman; dna replication; polymerase chain reaction; dna repair; protein interaction; trans-activators; helicase; dna primers; okazaki fragment; single stranded dna; dna binding; enzyme specificity; enzyme structure; genetic code; dna, bacterial; dna helicases; escherichia coli proteins; replication fork; protein pria; dna b; non-replicative helicases; protein uvrd |
| Journal Title: | DNA Repair |
| Volume: | 6 |
| Issue: | 7 |
| ISSN: | 1568-7864 |
| Publisher: | Elsevier Inc. |
| Date Published: | 2007-07-01 |
| Start Page: | 945 |
| End Page: | 952 |
| Language: | English |
| DOI: | 10.1016/j.dnarep.2007.02.014 |
| PUBMED: | 17382604 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 18" - "Export Date: 17 November 2011" - "CODEN: DRNEA" - "Source: Scopus" |
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