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Gene Review

priA  -  Primosome factor n' (replication factor Y)

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3927, JW3906, srgA
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Disease relevance of priA

  • The priA gene encoding the primosomal replicative n' protein of Escherichia coli [1].
  • Enhanced overproduction of greater than 1000-fold was achieved by replacing the natural Shine-Dalgarno sequence with that of the phage T7 phi 10 gene and placing this priA under the control of the T7 phage promoter and RNA polymerase [1].
  • Homologues of helicase genes priA and ruvAB of Borrelia burgdorferi, the Lyme borreliosis agent [2].
  • In vivo, the priA mutant fails to produce phi X174 phage and, remarkably, is unable to maintain plasmids that depend on the E. coli chromosome origin as well as those of ColE1 [3].
  • To investigate the role of PriA in recombination and repair in Neisseria gonorrhoeae, we identified, cloned, and insertionally inactivated the gonococcal priA homologue [4].

High impact information on priA

  • It is also essential for growth of a strain lacking PriA, indicating that it might affect replication fork progression or fork rescue. dnaC suppressors of priA overcome this inviability, especially when RecF, RecO or RecR is inactivated, indicating that RdgC avoids or counters a toxic effect of these proteins [5].
  • In both cases, SDR is restored by introduction of a plasmid carrying a wild-type priA gene [6].
  • Lastly, it was tested whether the ability to resolve chromosome dimers caused by XOs was important in a priA mutant by mutating dif and the C-terminal portion of ftsK [7].
  • The phenotypes of priA null mutations suggest that the protein participates in replication restart at recombination intermediates [8].
  • Molecular cloning and DNA sequence analysis of Escherichia coli priA, the gene encoding the primosomal protein replication factor Y [9].

Chemical compound and disease context of priA


Biological context of priA

  • Soluble protein extracts from cells harboring the priA gene on a multicopy plasmid contained 45-fold more n' replication activity than wild-type extracts [1].
  • The recF and priA genes have roles in DNA repair and homologous recombination [11].
  • DnaC809, a priA suppressor, failed to allow priA or priB mutants to grow using cSDR to initiate DNA replication [12].
  • Two subtle priA missense mutations either eliminated the ability to grow using cSDR (priA301 C479Y) or resulted in very small colonies (priA300 K230R) [12].
  • In a wild-type background, the three priA mutations had little, if any, effect on the phenotypes of UV resistance, basal levels of SOS expression and cell viability [13].

Anatomical context of priA


Associations of priA with chemical compounds

  • Cells deleted for the polA (DNA polymerase I) or priA (primosome) genes are as sensitive to MMS and MNNG as alkA tag bacteria [14].
  • The priA mutant was also more sensitive to the oxidative damaging agents H2O2 and cumene hydroperoxide compared to the parental strain [4].
  • The priA gene of the basidiomycete Lentinus edodes possesses a pyrimidine (CT)-rich stretch (26 bp) that includes a short (6-bp) repeat, the elements of which form a mirror repeat at and near the transcriptional initiation sites [15].
  • The sensitivity of priA mutants to cisplatin is also consistent with this conclusion [16].

Other interactions of priA

  • Unlike other dnaC suppressors, it can only weakly suppress the absence of priA [17].
  • (CAG)n.(CTG)n deletion rates were decreased, relative to the rates in wild type cells, in strains containing mutations in priA, recG, ruvAB, and recO [18].
  • Expression of the B. burgdorferi ruvB and ruvA genes renders a wild-type Escherichia coli sensitive to UV light and mitomycin, indicative of negative complementation. priA, which encodes the potential recognition factor for the primosome assembly site, was found at 15 kbp from the left telomere [2].
  • In the priC mutant, all three priA mutations behaved similarly, producing little, if any, changes in phenotypes [13].
  • Suppressors of this phenotype, called srgA, were located close to metB and shown to be alleles of priA [19].


  1. The priA gene encoding the primosomal replicative n' protein of Escherichia coli. Lee, E.H., Masai, H., Allen, G.C., Kornberg, A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  2. Homologues of helicase genes priA and ruvAB of Borrelia burgdorferi, the Lyme borreliosis agent. Boursaux-Eude, C., Margarita, D., Belfaiza, J., Old, I.G., Saints Girons, I. Res. Microbiol. (1998) [Pubmed]
  3. Replication deficiencies in priA mutants of Escherichia coli lacking the primosomal replication n' protein. Lee, E.H., Kornberg, A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  4. Mutation of the priA gene of Neisseria gonorrhoeae affects DNA transformation and DNA repair. Kline, K.A., Seifert, H.S. J. Bacteriol. (2005) [Pubmed]
  5. The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA. Moore, T., McGlynn, P., Ngo, H.P., Sharples, G.J., Lloyd, R.G. EMBO J. (2003) [Pubmed]
  6. Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication. Masai, H., Asai, T., Kubota, Y., Arai, K., Kogoma, T. EMBO J. (1994) [Pubmed]
  7. Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant. McCool, J.D., Sandler, S.J. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Replication fork assembly at recombination intermediates is required for bacterial growth. Liu, J., Xu, L., Sandler, S.J., Marians, K.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  9. Molecular cloning and DNA sequence analysis of Escherichia coli priA, the gene encoding the primosomal protein replication factor Y. Nurse, P., DiGate, R.J., Zavitz, K.H., Marians, K.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  10. The integrative transformation of Pleurotus ostreatus using bialaphos resistance as a dominant selectable marker. Yanai, K., Yonekura, K., Usami, H., Hirayama, M., Kajiwara, S., Yamazaki, T., Shishido, K., Adachi, T. Biosci. Biotechnol. Biochem. (1996) [Pubmed]
  11. Overlapping functions for recF and priA in cell viability and UV-inducible SOS expression are distinguished by dnaC809 in Escherichia coli K-12. Sandler, S.J. Mol. Microbiol. (1996) [Pubmed]
  12. Requirements for replication restart proteins during constitutive stable DNA replication in Escherichia coli K-12. Sandler, S.J. Genetics (2005) [Pubmed]
  13. PriA mutations that affect PriA-PriC function during replication restart. Sandler, S.J., McCool, J.D., Do, T.T., Johansen, R.U. Mol. Microbiol. (2001) [Pubmed]
  14. Homologous recombination prevents methylation-induced toxicity in Escherichia coli. Nowosielska, A., Smith, S.A., Engelward, B.P., Marinus, M.G. Nucleic Acids Res. (2006) [Pubmed]
  15. Structure and function of a pyrimidine/purine-biased sequence from the 5'-flanking region of the basidiomycete Lentinus edodes gene priA. Yamazaki, T., Hasebe, T., Kajiwara, S., Shishido, K. Mol. Gen. Genet. (2000) [Pubmed]
  16. Cisplatin induces DNA double-strand break formation in Escherichia coli dam mutants. Nowosielska, A., Marinus, M.G. DNA Repair (Amst.) (2005) [Pubmed]
  17. A novel dnaC mutation that suppresses priB rep mutant phenotypes in Escherichia coli K-12. Boonsombat, R., Yeh, S.P., Milne, A., Sandler, S.J. Mol. Microbiol. (2006) [Pubmed]
  18. Replication restart: a pathway for (CTG).(CAG) repeat deletion in Escherichia coli. Kim, S.H., Pytlos, M.J., Sinden, R.R. Mutat. Res. (2006) [Pubmed]
  19. Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12. Al-Deib, A.A., Mahdi, A.A., Lloyd, R.G. J. Bacteriol. (1996) [Pubmed]
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