D
IPR041222

Primosomal protein N', 3' DNA-binding domain

InterPro entry
Short namePriA_3primeBD
Overlapping
homologous
superfamilies
 

Description

This domain represents the N-terminal DNA-binding domain found in the PriA protein. This domain has been shown to bind the 3' end of the leading-strand arm of replication fork structures
[2, 1]
.

Primosomal protein N', also known as ATP-dependent helicase PriA, is a component of the primosome, which is involved in replication, repair, and recombination. PriA serves as a sensor/stabiliser for an arrested replication fork and eventually promotes restart of DNA replication through assembly of a primosome. It also serves as a checkpoint protein that prevents the replicase from advancing in a strand displacement reaction on forks that do not contain a functional replicative helicase
[3, 4]
.

References

1.Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA. Sasaki K, Ose T, Okamoto N, Maenaka K, Tanaka T, Masai H, Saito M, Shirai T, Kohda D. EMBO J. 26, 2584-93, (2007). View articlePMID: 17464287

2.Structural mechanisms of PriA-mediated DNA replication restart. Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel SR, Sandler SJ, Ha T, Keck JL. Proc. Natl. Acad. Sci. U.S.A. 111, 1373-8, (2014). View articlePMID: 24379377

3.Escherichia coli PriA protein, two modes of DNA binding and activation of ATP hydrolysis. Tanaka T, Mizukoshi T, Sasaki K, Kohda D, Masai H. J. Biol. Chem. 282, 19917-27, (2007). View articlePMID: 17483094

4.The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity. Manhart CM, McHenry CS. J. Biol. Chem. 288, 3989-99, (2013). View articlePMID: 23264623

GO terms

biological process

  • None

molecular function

cellular component

  • None

Cross References

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.