Inhibitory effect of UvrD and DinG on the replication of ColE1-derived plasmids in Escherichia coli

Kang, Nalae; Choi, Eunsil; Kim, Sung-Gun; Hwang, Jihwan

doi:10.1016/j.plasmid.2015.06.002

Cited by 2 publications

(2 citation statements)

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“…UvrD is a superfamily 1 helicase that translocates 3'-5' along ssDNA. The ability of UvrD to compensate partially for the absence of Rep has been attributed to the high degree of homology between these two helicases and the abundance of UvrD inside cells (12,21,(37)(38)(39). The role of UvrD in nucleotide excision repair along with UvrABC proteins as well as in methyl-directed mismatch repair along with the MutHLS proteins is well characterised (40)(41)(42)(43)(44)(45).…”

Section: Introductionmentioning

confidence: 99%

“…Rep is the primary accessory helicase in E. coli, however, UvrD, a superfamily 1 helicase that translocates 3'-5' along ssDNA, partially compensates for its absence in vivo, attributed to the high degree of homology between these two helicases and the abundance of UvrD inside cells (12,21,(36)(37)(38). Rep also promotes replication through stalled transcription elongation complexes (1,12,13,39,40).…”

Section: Introductionmentioning

confidence: 99%

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Tetrameric UvrD helicase is located at theE. colireplisome due to frequent replication blocks

Wollman

Syeda

Leech

et al. 2021

Preprint

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DNA replication in all organisms must overcome nucleoprotein blocks to complete genome duplication. Accessory replicative helicases in Escherichia coli, Rep and UvrD, help replication machinery overcome blocks by removing incoming nucleoprotein complexes or aiding the re-initiation of replication. Mechanistic details of Rep function have emerged from recent live cell studies, however, the activities of UvrD in vivo remain unclear. Here, by integrating biochemical analysis and super-resolved single-molecule fluorescence microscopy, we discovered that UvrD self-associates into a tetramer and, unlike Rep, is not recruited to a specific replisome protein despite being found at approximately 80% of replication forks. By deleting rep and DNA repair factors mutS and uvrA, perturbing transcription by mutating RNA polymerase, and antibiotic inhibition; we show that the presence of UvrD at the fork is dependent on its activity. This is likely mediated by the very high frequency of replication blocks due to DNA bound proteins, including RNA polymerase, and DNA damage. UvrD is recruited to sites of nucleoprotein blocks via distinctly different mechanisms to Rep and therefore plays a more important and complementary role than previously realised in ensuring successful DNA replication.

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