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Gene Review

dnaC  -  DNA biosynthesis protein

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4351, JW4325, dnaD
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Disease relevance of dnaC


High impact information on dnaC

  • DNA biosynthesis subsequent to all three events will generate predominantly O6-meG X T base pairs as O6meG preferentially pairs with T [4].
  • 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].
  • The gene is located adjacent to the dnaC locus, probably both being in a single operon [6].
  • The P-14 gene is transcribed from an upstream promoter, and its transcript extends through dnaT and dnaC [7].
  • Similar to dnaG and dnaT, dnaC uses several minor codons; the significance of these minor codons to the low level expression of the protein product in E. coli cells remains to be determined [8].

Chemical compound and disease context of dnaC


Biological context of dnaC


Associations of dnaC with chemical compounds


Physical interactions of dnaC

  • Present studies demonstrate that the dnaC gene product binds ribonucleotides independent of dnaB protein [10].

Other interactions of dnaC

  • Others have reported a different type of dnaC mutation, dnaC1331, is able to mimic priB mutant phenotypes [1].
  • Unlike other dnaC suppressors, it can only weakly suppress the absence of priA [1].
  • An upstream open reading frame, separated by just 2 base pairs from the coding region of dnaC, encodes the COOH-terminal half of the dnaT product (protein i; Masai, H., Bond, M. W., and Arai, K. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 1256-1260) [8].

Analytical, diagnostic and therapeutic context of dnaC


  1. 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]
  2. Novel replication mutant of microvirid phage alpha 3 deleted in the complementary strand origin. Kodaira, K., Nakano, K., Taketo, A. Mol. Gen. Genet. (1990) [Pubmed]
  3. The Bacillus subtilis dnaC gene encodes a protein homologous to the DnaB helicase of Escherichia coli. Sakamoto, Y., Nakai, S., Moriya, S., Yoshikawa, H., Ogasawara, N. Microbiology (Reading, Engl.) (1995) [Pubmed]
  4. Mechanism of mutagenesis by O6-methylguanine. Eadie, J.S., Conrad, M., Toorchen, D., Topal, M.D. Nature (1984) [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. Cloning of the Escherichia coli gene for primosomal protein i: the relationship to dnaT, essential for chromosomal DNA replication. Masai, H., Bond, M.W., Arai, K. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  7. Operon structure of dnaT and dnaC genes essential for normal and stable DNA replication of Escherichia coli chromosome. Masai, H., Arai, K. J. Biol. Chem. (1988) [Pubmed]
  8. Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein. Nakayama, N., Bond, M.W., Miyajima, A., Kobori, J., Arai, K. J. Biol. Chem. (1987) [Pubmed]
  9. Mode of action of the dual-action cephalosporin Ro 23-9424. Georgopapadakou, N.H., Bertasso, A., Chan, K.K., Chapman, J.S., Cleeland, R., Cummings, L.M., Dix, B.A., Keith, D.D. Antimicrob. Agents Chemother. (1989) [Pubmed]
  10. Regulation of dnaB function in DNA replication in Escherichia coli by dnaC and lambda P gene products. Biswas, S.B., Biswas, E.E. J. Biol. Chem. (1987) [Pubmed]
  11. Low-level resistance to the cephalosporin 3'-quinolone ester Ro 23-9424 in Escherichia coli. Chapman, J.S., Bertasso, A., Cummings, L.M., Georgopapadakou, N.H. Antimicrob. Agents Chemother. (1995) [Pubmed]
  12. Monocyclic and tricyclic analogs of quinolones: mechanism of action. Georgopapadakou, N.H., Dix, B.A., Angehrn, P., Wick, A., Olson, G.L. Antimicrob. Agents Chemother. (1987) [Pubmed]
  13. Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Schmidt, A., Wu, H., MacKenzie, R.E., Chen, V.J., Bewly, J.R., Ray, J.E., Toth, J.E., Cygler, M. Biochemistry (2000) [Pubmed]
  14. Oxygen and redox-active drugs: shared toxicity sites. Brown, O.R., Seither, R.L. Fundamental and applied toxicology : official journal of the Society of Toxicology. (1983) [Pubmed]
  15. Characterization of dnaC2 and dnaC28 mutants by flow cytometry. Withers, H.L., Bernander, R. J. Bacteriol. (1998) [Pubmed]
  16. Mutants of bacteriophage T4 deficient in the ability to induce nuclear disruption: shutoff of host DNA and protein synthesis gene dosage experiments, identification of a restrictive host, and possible biological significance. Snustad, D.P., Bursch, C.J., Parson, K.A., Hefeneider, S.H. J. Virol. (1976) [Pubmed]
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