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
. 1973 Aug;70(8):2420–2423. doi: 10.1073/pnas.70.8.2420

The Synthesis In Vitro of RNA Polymerase Subunits of Escherichia coli

Stuart Austin 1, Duncan McGeoch 1
PMCID: PMC433748  PMID: 4365378

Abstract

DNA from transducing bacteriophage that carry the structural gene for the β subunit of RNA polymerase has been used to direct protein synthesis in a cell-free transcription-translation system. A polypeptide species has been detected which appears to be β-subunit material made in vitro.

Keywords: cell-free protein synthesis

Full text

PDF
2420

Selected References

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

  1. Burgess R. R. RNA polymerase. Annu Rev Biochem. 1971;40:711–740. doi: 10.1146/annurev.bi.40.070171.003431. [DOI] [PubMed] [Google Scholar]
  2. Burgess R. R. Separation and characterization of the subunits of ribonucleic acid polymerase. J Biol Chem. 1969 Nov 25;244(22):6168–6176. [PubMed] [Google Scholar]
  3. Burgess R. R., Travers A. A., Dunn J. J., Bautz E. K. Factor stimulating transcription by RNA polymerase. Nature. 1969 Jan 4;221(5175):43–46. doi: 10.1038/221043a0. [DOI] [PubMed] [Google Scholar]
  4. Chambers D. A., Zubay G. The stimulatory effect of cyclic adenosine 3'5'-monophosphate on DNA-directed synthesis of beta-galactosidase in a cell-free system. Proc Natl Acad Sci U S A. 1969 May;63(1):118–122. doi: 10.1073/pnas.63.1.118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. De Crombrugghe B., Chen B., Gottesman M., Pastan I., Varmus H. E., Emmer M., Perlman R. L. Regulation of lac mRNA synthesis in a soluble cell-free system. Nat New Biol. 1971 Mar 10;230(10):37–40. doi: 10.1038/newbio230037a0. [DOI] [PubMed] [Google Scholar]
  6. DeVries J. K., Zubay G. Characterization of a beta-galactosidase formed between a complementary protein and a peptide synthesized de novo. J Bacteriol. 1969 Mar;97(3):1419–1425. doi: 10.1128/jb.97.3.1419-1425.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eron L., Block R. Mechanism of initiation and repression of in vitro transcription of the lac operon of Escherichia coli. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1828–1832. doi: 10.1073/pnas.68.8.1828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Greenblatt J., Schleif R. Arabinose C protein: regulation of the arabinose operon in vitro. Nat New Biol. 1971 Oct 6;233(40):166–170. doi: 10.1038/newbio233166a0. [DOI] [PubMed] [Google Scholar]
  9. Heil A., Zillig W. Reconstitution of bacterial DNA-dependent RNA-polymerase from isolated subunits as a tool for the elucidation of the role of the subunits in transcription. FEBS Lett. 1970 Dec;11(3):165–168. doi: 10.1016/0014-5793(70)80519-1. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Marshall S., Gillespie D. New rifampin-resistant mutant of Escherichia coli. J Bacteriol. 1972 May;110(2):782–783. doi: 10.1128/jb.110.2.782-783.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Matzura H., Molin S., Maaloe O. Sequential biosynthesis of the and ' subunits of the DNA-dependent RNA polymerase from Escherichia coli. J Mol Biol. 1971 Jul 14;59(1):17–25. doi: 10.1016/0022-2836(71)90410-4. [DOI] [PubMed] [Google Scholar]
  13. Nomura M., Engbaek F. Expression of ribosomal protein genes as analyzed by bacteriophage Mu-induced mutations. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1526–1530. doi: 10.1073/pnas.69.6.1526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Parks J. S., Gottesman M., Perlman R. L., Pastan I. Regulation of galactokinase synthesis by cyclic adenosine 3',5'-monophosphate in cell-free extracts of Escherichia coli. J Biol Chem. 1971 Apr 25;246(8):2419–2424. [PubMed] [Google Scholar]
  15. Sippel A., Hartmann G. Mode of action of rafamycin on the RNA polymerase reaction. Biochim Biophys Acta. 1968 Mar 18;157(1):218–219. doi: 10.1016/0005-2787(68)90286-4. [DOI] [PubMed] [Google Scholar]
  16. Taylor A. L. Current linkage map of Escherichia coli. Bacteriol Rev. 1970 Jun;34(2):155–175. doi: 10.1128/br.34.2.155-175.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Yamamoto K. R., Alberts B. M., Benzinger R., Lawhorne L., Treiber G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology. 1970 Mar;40(3):734–744. doi: 10.1016/0042-6822(70)90218-7. [DOI] [PubMed] [Google Scholar]
  18. Zubay G., Gielow L., Englesberg E. Cell-free studies on the regulation of the arabinose operon. Nat New Biol. 1971 Oct 6;233(40):164–165. doi: 10.1038/newbio233164a0. [DOI] [PubMed] [Google Scholar]
  19. Zubay G., Morse D. E., Schrenk W. J., Miller J. H. Detection and isolation of the repressor protein for the tryptophan operon of Escherichia coli. Proc Natl Acad Sci U S A. 1972 May;69(5):1100–1103. doi: 10.1073/pnas.69.5.1100. [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