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Comment
. 2013 Dec;14(12):1032-3.
doi: 10.1038/embor.2013.171. Epub 2013 Nov 5.

Human Primpol1: a novel guardian of stalled replication forks

Jun-Sub Im  1 , Kyung Yong Lee, Laura W Dillon, Anindya Dutta
Affiliations
Comment

Human Primpol1: a novel guardian of stalled replication forks

Jun-Sub Im et al. EMBO Rep. 2013 Dec.
No abstract available

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Conflict of interest statement

The authors declare that they have no conflict of interest.

Figures

Figure 1
Figure 1
The role of hPrimpol1 in stalled replication fork restart. (A) Under normal conditions, the replicative helicase unwinds parental DNA, generating ssDNA that is coated by RPA and serves as a template for leading and lagging strand synthesis. Aside from interacting with RPA bound to the short stretches of ssDNA, the role of hPrimpol1 in normal progression of replication forks is unknown. (B) Following repair of a stalled replication fork, (1) hPrimpol1 rapidly resumes DNA synthesis of long stretches of RPA-coated ssDNA located at the stalled fork site. Later, the leading-strand polymerase (2) or lagging-strand primase and polymerase (3) replace hPrimpol1 to complete replication of genomic DNA. RPA, replication protein A; ssDNA, single-stranded DNA.
See this image and copyright information in PMC

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