Skip to main content
PMC home page
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
. 1980 Apr;77(4):1991–1994. doi: 10.1073/pnas.77.4.1991

L factor that is required for beta-galactosidase synthesis is the nusA gene product involved in transcription termination.

J Greenblatt, J Li, S Adhya, D I Friedman, L S Baron, B Redfield, H F Kung, H Weissbach
PMCID: PMC348636  PMID: 6154941

Abstract

The DNA-dependent in vitro synthesis of Escherichia coli beta-galactosidase requires the presence of a soluble protein referred to as L factor [Kung, H., Spears, C. & Weissbach, H. (1975) J. Biol. Chem. 250, 1556-1562]. In the present study, comparison of physical, immunological, and biological properties shows that L factor is the product of the E. coli nusA gene. The nusA gene product is known to interact with bacteriophage lambda N gene protein and to prevent premature termination of transcription from the early lambda promoters. Our results suggest that premature transcription termination in the lac operon of E. coli may also be overcome by the nusA protein.

Full text

PDF
1993

Images in this article

1992Image
on p.1992

Selected References

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

  1. Adhya S., Gottesman M., De Crombrugghe B. Release of polarity in Escherichia coli by gene N of phage lambda: termination and antitermination of transcription. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2534–2538. doi: 10.1073/pnas.71.6.2534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adhya S., Miller W. Modulation of the two promoters of the galactose operon of Escherichia coli. Nature. 1979 Jun 7;279(5713):492–494. doi: 10.1038/279492a0. [DOI] [PubMed] [Google Scholar]
  3. Barry G., Squires C. L., Squires C. Control features within the rplJL-rpoBC transcription unit of Escherichia coli. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4922–4926. doi: 10.1073/pnas.76.10.4922. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. De Crombrugghe B., Adhya S., Gottesman M., Pastan I. Effect of Rho on transcription of bacterial operons. Nat New Biol. 1973 Feb 28;241(113):260–264. doi: 10.1038/newbio241260a0. [DOI] [PubMed] [Google Scholar]
  5. Franklin N. C. Altered reading of genetic signals fused to the N operon of bacteriophage lambda: genetic evidence for modification of polymerase by the protein product of the N gene. J Mol Biol. 1974 Oct 15;89(1):33–48. doi: 10.1016/0022-2836(74)90161-2. [DOI] [PubMed] [Google Scholar]
  6. Friedman D. I., Baumann M., Baron L. S. Cooperative effects of bacterial mutations affecting lambda N gene expression. I. Isolation and characterization of a nusB mutant. Virology. 1976 Aug;73(1):119–127. doi: 10.1016/0042-6822(76)90066-0. [DOI] [PubMed] [Google Scholar]
  7. Friedman D. I., Jolly C. T., Mural R. J. Interference with the expression of the N gene function of phage lambda in a mutant of Escherichia coli. Virology. 1973 Jan;51(1):216–226. doi: 10.1016/0042-6822(73)90381-4. [DOI] [PubMed] [Google Scholar]
  8. Friedman D. I., Wilgus G. S., Mural R. J. Gene N regulator function of phage lambda immun21: evidence that a site of N action differs from a site of N recognition. J Mol Biol. 1973 Dec 25;81(4):505–516. doi: 10.1016/0022-2836(73)90519-6. [DOI] [PubMed] [Google Scholar]
  9. Greenblatt J., Malnoe P., Li J. Purification of the gene N transcription anti-termination protein of bacteriophage lambda. J Biol Chem. 1980 Feb 25;255(4):1465–1470. [PubMed] [Google Scholar]
  10. Kung H. F., Redfield B., Treadwell B. V., Eskin B., Spears C., Weissbach H. DNA-directed in vitro synthesis of beta-galactosidase. Studies with purified factors. J Biol Chem. 1977 Oct 10;252(19):6889–6894. [PubMed] [Google Scholar]
  11. Kung H., Spears C., Weissbach H. Purification and properties of a soluble factor required for the deoxyribonucleic acid-directed in vitro synthesis of beta-galactosidase. J Biol Chem. 1975 Feb 25;250(4):1556–1562. [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [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. Lozeron H. A., Anevski P. J., Apirion D. Antitermination and absence of processing of the leftward transcript of coliphage lambda in the RNAase III-deficient host. J Mol Biol. 1977 Jan 15;109(2):359–365. doi: 10.1016/s0022-2836(77)80039-9. [DOI] [PubMed] [Google Scholar]
  15. Luzzati D. Regulation of lambda exonuclease synthesis: role of the N gene product and lambda repressor. J Mol Biol. 1970 Apr 28;49(2):515–519. doi: 10.1016/0022-2836(70)90261-5. [DOI] [PubMed] [Google Scholar]
  16. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  17. Roberts J. W. Termination factor for RNA synthesis. Nature. 1969 Dec 20;224(5225):1168–1174. doi: 10.1038/2241168a0. [DOI] [PubMed] [Google Scholar]
  18. Segawa T., Imamoto F. Diversity of regulation of genetic transcription. II. Specific relaxation of polarity in read-through transcription of the translocated trp operon in bacteriophage lambda trp. J Mol Biol. 1974 Aug 25;87(4):741–754. doi: 10.1016/0022-2836(74)90082-5. [DOI] [PubMed] [Google Scholar]
  19. Ullmann A., Joseph E., Danchin A. Cyclic AMP as a modulator of polarity in polycistronic transcriptional units. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3194–3197. doi: 10.1073/pnas.76.7.3194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Zarucki-Schulz T., Jerez C., Goldberg G., Kung H. F., Huang K. H., Brot N., Weissbach H. DNA-directed in vitro synthesis of proteins involved in bacterial transcription and translation. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6115–6119. doi: 10.1073/pnas.76.12.6115. [DOI] [PMC free article] [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