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. 1982 Aug;151(2):918–923. doi: 10.1128/jb.151.2.918-923.1982

Regulation of tryptophanyl-tRNA synthetase formation.

C V Hall, C Yanofsky
PMCID: PMC220343  PMID: 7047500

Abstract

A previously constructed trp-S-lacZ fusion encoding a hybrid protein with beta-galactosidase activity was subcloned from a multicopy plasmid onto a lambda vector. Single-copy lysogens of lambda trpS-lacZ were used to determine whether trpS was regulated in a manner similar to that of other aminoacyl-tRNA synthetases. trpS regulation was found to resemble that of the majority of synthetases, in that expression of the lysogen-encoded hybrid beta-galactosidase varied with growth rate; beta-galactosidase activity increased 2.5-fold as the generation time decreased from 150 to 37 min. This regulatory response was confirmed by DNA/RNA hybridization experiments, which also suggested that this form of metabolic regulation occurred at the transcriptional level. No alteration in the level of hybrid beta-galactosidase was observed, however, when cells were starved for tryptophan.

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Selected References

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

  1. Baer M., Low K. B., Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase. J Bacteriol. 1979 Jul;139(1):165–175. doi: 10.1128/jb.139.1.165-175.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barry G., Squires C., Squires C. L. Attenuation and processing of RNA from the rplJL--rpoBC transcription unit of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3331–3335. doi: 10.1073/pnas.77.6.3331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berk A. J., Sharp P. A. Sizing and mapping of early adenovirus mRNAs by gel electrophoresis of S1 endonuclease-digested hybrids. Cell. 1977 Nov;12(3):721–732. doi: 10.1016/0092-8674(77)90272-0. [DOI] [PubMed] [Google Scholar]
  4. Borck K., Beggs J. D., Brammar W. J., Hopkins A. S., Murray N. E. The construction in vitro of transducing derivatives of phage lambda. Mol Gen Genet. 1976 Jul 23;146(2):199–207. doi: 10.1007/BF00268089. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Casadaban M. J., Cohen S. N. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol. 1980 Apr;138(2):179–207. doi: 10.1016/0022-2836(80)90283-1. [DOI] [PubMed] [Google Scholar]
  7. Clarke S. J., Low B., Konigsberg W. Isolation and characterization of a regulatory mutant of an aminoacyl-transfer ribonucleic acid synthetase in Escherichia coli K-12. J Bacteriol. 1973 Mar;113(3):1096–1103. doi: 10.1128/jb.113.3.1096-1103.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Eisenberg S. P., Yarus M., Soll L. The effect of an Escherichia coli regulatory mutation on transfer RNA structure. J Mol Biol. 1979 Nov 25;135(1):111–126. doi: 10.1016/0022-2836(79)90343-7. [DOI] [PubMed] [Google Scholar]
  9. Gunsalus R. P., Zurawski G., Yanofsky C. Structural and functional analysis of cloned deoxyribonucleic acid containing the trpR-thr region of the Escherichia coli chromosome. J Bacteriol. 1979 Oct;140(1):106–113. doi: 10.1128/jb.140.1.106-113.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hall C. V., Yanofsky C. Cloning and characterization of the gene for Escherichia coli tryptophanyl-transfer ribonucleic acid synthetase. J Bacteriol. 1981 Dec;148(3):941–949. doi: 10.1128/jb.148.3.941-949.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LaRossa R., Vögell G., Low K. B., Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli. II. Isolation of regulatory mutants affecting leucyl-tRNA synthetase levels. J Mol Biol. 1977 Dec 25;117(4):1033–1048. doi: 10.1016/s0022-2836(77)80011-9. [DOI] [PubMed] [Google Scholar]
  12. McGinnis E., Williams L. S. Regulation of histidyl-transfer ribonucleic acid synthetase formation in a histidyl-transfer ribonucleic acid synthetase mutant of Salmonella typhimurium. J Bacteriol. 1972 Sep;111(3):739–744. doi: 10.1128/jb.111.3.739-744.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Miura A., Krueger J. H., Itoh S., de Boer H. A., Nomura M. Growth-rate-dependent regulation of ribosome synthesis in E. coli: expression of the lacZ and galK genes fused to ribosomal promoters. Cell. 1981 Sep;25(3):773–782. doi: 10.1016/0092-8674(81)90185-9. [DOI] [PubMed] [Google Scholar]
  14. Morgan S. D., Söll D. Regulation of the biosynthesis of aminoacid: tRNA ligases and of tRNA. Prog Nucleic Acid Res Mol Biol. 1978;21:181–207. doi: 10.1016/s0079-6603(08)60270-6. [DOI] [PubMed] [Google Scholar]
  15. Morse D. E., Morse A. N. Dual-control of the tryptophan operon is mediated by both tryptophanyl-tRNA synthetase and the repressor. J Mol Biol. 1976 May 15;103(2):209–226. doi: 10.1016/0022-2836(76)90310-7. [DOI] [PubMed] [Google Scholar]
  16. Neidhardt F. C., Bloch P. L., Pedersen S., Reeh S. Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J Bacteriol. 1977 Jan;129(1):378–387. doi: 10.1128/jb.129.1.378-387.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Neihardt F. C., Parker J., McKeever W. G. Function and regulation of aminoacyl-tRNA synthetases in prokaryotic and eukaryotic cells. Annu Rev Microbiol. 1975;29:215–250. doi: 10.1146/annurev.mi.29.100175.001243. [DOI] [PubMed] [Google Scholar]
  18. OTSUJI N., SEKIGUCHI M., IIJIMA T., TAKAGI Y. Induction of phage formation in the lysogenic Escherichia coli K-12 by mitomycin C. Nature. 1959 Oct 3;184(Suppl 14):1079–1080. doi: 10.1038/1841079b0. [DOI] [PubMed] [Google Scholar]
  19. Putney S. D., Schimmel P. An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription. Nature. 1981 Jun 25;291(5817):632–635. doi: 10.1038/291632a0. [DOI] [PubMed] [Google Scholar]
  20. Reeh S., Pedersen S., Neidhardt F. C. Transient rates of synthesis of five amionacyl-transfer ribonucleic acid synthetases during a shift-up of Escherichia coli. J Bacteriol. 1977 Feb;129(2):702–706. doi: 10.1128/jb.129.2.702-706.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Reiser J., Renart J., Stark G. R. Transfer of small DNA fragments from polyacrylamide gels to diazobenzyloxymethyl-paper and detection by hybridization with DNA probes. Biochem Biophys Res Commun. 1978 Dec 14;85(3):1104–1112. doi: 10.1016/0006-291x(78)90656-3. [DOI] [PubMed] [Google Scholar]
  22. Sakonju S., Bogenhagen D. F., Brown D. D. A control region in the center of the 5S RNA gene directs specific initiation of transcription: I. The 5' border of the region. Cell. 1980 Jan;19(1):13–25. doi: 10.1016/0092-8674(80)90384-0. [DOI] [PubMed] [Google Scholar]
  23. Schimmel P. R., Söll D. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu Rev Biochem. 1979;48:601–648. doi: 10.1146/annurev.bi.48.070179.003125. [DOI] [PubMed] [Google Scholar]
  24. Selker E., Yanofsky C. Nucleotide sequence of the trpC-trpB intercistronic region from Salmonella typhimurium. J Mol Biol. 1979 May 15;130(2):135–143. doi: 10.1016/0022-2836(79)90422-4. [DOI] [PubMed] [Google Scholar]
  25. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  26. Theall G., Low K. B., Söll D. Regulation of the biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli. IV. Mutants with increased levels of leucyl- or seryl-tRNA synthetase. Mol Gen Genet. 1979 Jan 31;169(2):205–211. doi: 10.1007/BF00271672. [DOI] [PubMed] [Google Scholar]
  27. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  28. Yanofsky C. Attenuation in the control of expression of bacterial operons. Nature. 1981 Feb 26;289(5800):751–758. doi: 10.1038/289751a0. [DOI] [PubMed] [Google Scholar]
  29. Yanofsky C. Mutations affecting tRNATrp and its charging and their effect on regulation of transcription termination at the attenuator of the tryptophan operon. J Mol Biol. 1977 Jul 15;113(4):663–677. doi: 10.1016/0022-2836(77)90229-7. [DOI] [PubMed] [Google Scholar]

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