Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1983 Aug;80(15):4659–4663. doi: 10.1073/pnas.80.15.4659

Identification of Escherichia coli DNA helicase I as the traI gene product of the F sex factor.

M Abdel-Monem, G Taucher-Scholz, M Q Klinkert
PMCID: PMC384103  PMID: 6308637

Abstract

Active DNA helicase I (Mr 180,000) can be isolated from Escherichia coli F+ strains but not F- strains. The transfer of the F sex factor to F- strains by conjugation permits the purification of the enzyme from the transconjugant strains. We conclude from this that helicase I is coded for by a portion of the F factor. Results also obtained by using recombinant plasmids carrying different DNA fragments of the F factor transfer region suggest that DNA helicase I is identical to the product of traI, one of the transfer genes of the F factor.

Full text

PDF
4659

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abdel-Monem M., Dürwald H., Hoffmann-Berling H. DNA unwinding enzyme II of Escherichia coli. 2. Characterization of the DNA unwinding activity. Eur J Biochem. 1977 Sep 15;79(1):39–45. doi: 10.1111/j.1432-1033.1977.tb11781.x. [DOI] [PubMed] [Google Scholar]
  2. Abdel-Monem M., Dürwald H., Hoffmann-Berling H. Enzymic unwinding of DNA. 2. Chain separation by an ATP-dependent DNA unwinding enzyme. Eur J Biochem. 1976 Jun 1;65(2):441–449. doi: 10.1111/j.1432-1033.1976.tb10359.x. [DOI] [PubMed] [Google Scholar]
  3. Abdel-Monem M., Hoffmann-Berling H. Enzymic unwinding of DNA. 1. Purification and characterization of a DNA-dependent ATPase from Escherichia coli. Eur J Biochem. 1976 Jun 1;65(2):431–440. doi: 10.1111/j.1432-1033.1976.tb10358.x. [DOI] [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  5. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  6. Cohen S. N., Chang A. C., Hsu L. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2110–2114. doi: 10.1073/pnas.69.8.2110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Everett R., Willetts N. Characterisation of an in vivo system for nicking at the origin of conjugal DNA transfer of the sex factor F. J Mol Biol. 1980 Jan 15;136(2):129–150. doi: 10.1016/0022-2836(80)90309-5. [DOI] [PubMed] [Google Scholar]
  8. Geider K., Hoffmann-Berling H. Proteins controlling the helical structure of DNA. Annu Rev Biochem. 1981;50:233–260. doi: 10.1146/annurev.bi.50.070181.001313. [DOI] [PubMed] [Google Scholar]
  9. Johnson D. A., Willetts N. S. Construction and characterization of multicopy plasmids containing the entire F transfer region. Plasmid. 1980 Nov;4(3):292–304. doi: 10.1016/0147-619x(80)90068-2. [DOI] [PubMed] [Google Scholar]
  10. Kingsman A., Willetts N. The requirements for conjugal DNA synthesis in the donor strain during flac transfer. J Mol Biol. 1978 Jul 5;122(3):287–300. doi: 10.1016/0022-2836(78)90191-2. [DOI] [PubMed] [Google Scholar]
  11. Klinkert M. Q., Klein A., Abdel-Monem M. Studies on the functions of DNA helicase I and DNA helicase II of Escherichia coli. J Biol Chem. 1980 Oct 25;255(20):9746–9752. [PubMed] [Google Scholar]
  12. Kuhn B., Abdel-Monem M., Hoffmann-Berling H. DNA helicases. Cold Spring Harb Symp Quant Biol. 1979;43(Pt 1):63–67. doi: 10.1101/sqb.1979.043.01.011. [DOI] [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Manning P. A., Kusecek B., Morelli G., Fisseau C., Achtman M. Analysis of the promoter-distal region of the tra operon of the F sex factor of Escherichia coli K-12 encoded by EcoRI restriction fragments f17, f19, and f2. J Bacteriol. 1982 Apr;150(1):76–88. doi: 10.1128/jb.150.1.76-88.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Schweitzer S., Blohm D., Geider K. Expression of Ti-plasmid DNA in E. coli: comparison of homologous fragments cloned from Ti plasmids of Agrobacterium strains C58 and Ach5. Plasmid. 1980 Sep;4(2):196–204. doi: 10.1016/0147-619x(80)90009-8. [DOI] [PubMed] [Google Scholar]
  16. Scott J. F., Eisenberg S., Bertsch L. L., Kornberg A. A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: catalytic strand separation in advance of replication. Proc Natl Acad Sci U S A. 1977 Jan;74(1):193–197. doi: 10.1073/pnas.74.1.193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Skurray R. A., Nagaishi H., Clark A. J. Molecular cloning of DNA from F sex factor of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1976 Jan;73(1):64–68. doi: 10.1073/pnas.73.1.64. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Switzer R. C., 3rd, Merril C. R., Shifrin S. A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem. 1979 Sep 15;98(1):231–237. doi: 10.1016/0003-2697(79)90732-2. [DOI] [PubMed] [Google Scholar]
  19. Vogt V. M. Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae. Eur J Biochem. 1973 Feb 15;33(1):192–200. doi: 10.1111/j.1432-1033.1973.tb02669.x. [DOI] [PubMed] [Google Scholar]
  20. Yarranton G. T., Das R. H., Gefter M. L. Enzyme-catalyzed DNA unwinding. Mechanism of action of helicase III. J Biol Chem. 1979 Dec 10;254(23):12002–12006. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES