Skip to main content
SpringerLink
Log in

Strains of Escherichia coli carrying the structural gene for histidyl-tRNA synthetase on a high copy-number plasmid

  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Summary

That portion of the Escherichia coli chromosome caried by a number of lambda transducing phages, all of which carry the gua operon, wss mapped using restriction endonucleases. The DNA from one of these transducing phages was subcloned onto pBR322. We have identified two recombinant plasmids which carry the Escherichia coli gene hisS, the structural gene for histidyl-tRNA synthetase. The two plasmids, pSE301 and pSE401, have in common a 3,540 bp fragment of E. coli DNA which is bounded by BglII and SalI restriction endonuclease recognition sites. Strains carrying these plasmids overproduce histidyl-tRNA synthetase 20 to 30 fold. The growth rate of these strains is not affected although the histidine biosynthetic enzymes are derepressed. This derepression seems to be in addition to that caused by introduction of a hisT mutation on the chromosome.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Bachmann BJ, Low KB (1980) Linkage map of Escherichia coli K-12, edition 6. Microbiol Rev 44:1–56

    Google Scholar 

  • Barnes WM (1978) DNA sequence from the histidine operon control region: seven histidine codons in a row. Proc Natl Acad Sci USA 75:4281–4285

    Google Scholar 

  • Bloch PL, Phillips TA, Neidhardt FC (1980) Protein identification on O'Farrell two-dimensional gels: locations of 81 Escherichia coli proteins. J Bacteriol 141:1409–1420

    Google Scholar 

  • Bolivar F, Rodriquez RL, Greene PJ, Betlach MC, Heynecker HL, Boyer HW (1977) Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene 2:95–113

    Google Scholar 

  • Bruni CB, Colantuoni V, Sbordone L, Cortese R, Blasi F (1977) Biochemical and regulatory properties of Escherichia coli K-12 hisT mutants. J Bacteriol 130:4–10

    Google Scholar 

  • Chapeville F, Lipmann F, von Ehrenstein G, Weisblum B, Ray Jr WJ, Benzer S (1962) On the role of soluble ribonucleic acid in coding for amino acids. Proc Natl Acad Sci USA 48:1086–1092

    Google Scholar 

  • Clewell DB, Helinski DR (1970) Properties of a supercoiled deoxyribonucleic acid-protein relaxation complex and strand specificity of the relaxation event. Biochemistry 9:4440–4482

    Google Scholar 

  • Cortese R, Landsberg R, Vonder Haar RA, Umbarger HE, Ames BN (1974) Pleiotrophy of hisT mutants blocked in pseudouridine synthesis in tRNA: leucine and isoleucine-valine operons. Proc Natl Acad Sci USA 71:1857–1861

    Google Scholar 

  • DiNocera PP, Blasi F, DiLauro R, Frunzio R, Bruni CB (1978) Nucleotide sequence of the attenuator region of the histidine operon of Escherichia coli K-12. Proc Natl Acad Sci USA 75:4276–4280

    Google Scholar 

  • Fishman SE, Kerchief KR, Parker J (1979) Specialized lambda transducing bacteriophage which carries hisS, the structural gene for histidyl-transfer ribonucleic acid synthetase. J Bacteriol 139:404–410

    Google Scholar 

  • Johnson RC, Vanatta PR, Fresco JR (1977) Metabolic regulation of aminoacyl-tRNA synthetase biosynthesis in baker's yeast. J Biol Chem 252:878–882

    Google Scholar 

  • Johnston HM, Barnes WM, Chumley FG, Bossi L, Roth JR (1980) Model for regulation of the histidine operon of Salmonella. Proc Natl Acad Sci USA 77:508–512

    Google Scholar 

  • Lawther RP, Hatfield GW (1977) Biochemical characterization of Escherichia coli hisT strain. J Bacteriol 130:552–557

    Google Scholar 

  • Lennox ES (1955) Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1:190–206

    Google Scholar 

  • Leoning UE (1967) The fractionation of high molecular weight ribonucleic acid by polyacrylamide gel electrophoresis. Biochem J 102:251–257

    Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with folin phenol reagent. J Biol Chem 193:265–275

    Google Scholar 

  • Mandel M, Higa A (1970) Calcium-dependent bacteriophage DNA infection. J Mol Biol 73:453–471

    Google Scholar 

  • Martin RG, Berberich MA, Ames BN, Davis WW, Goldberger RF, Yourno JD (1971) Enzymes and intermediates of histidine biosynthesis in Salmonella typhimurium. Methods Enzymol 17:3–44

    Google Scholar 

  • McGinnis E, Williams LS (1972a) Role of histidine transfer ribonucleic acid in regulation of synthesis of histidyl-transfer ribonucleic acid synthetase of Salmonella typhimurium. J Bacteriol 109:505–511

    Google Scholar 

  • McGinnis E, Williams LS (1972b) Regulation of histidyl-transfer ribonucleic acid synthetase formation in a histidyl-transfer ribonucleic acid synthetase mutant of Salmonella typhimurium. J Bacteriol 111:739–744

    Google Scholar 

  • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY

    Google Scholar 

  • Murray ML, Hartman PE (1972) Overproduction of hisH and hisF gene products lead to inhibition of cell division in Salmonella. Can J Microbiol 18:671–681

    Google Scholar 

  • Nass G (1967) Regulation of histidine biosynthetic enzymes in a mutant of Escherichia coli with an altered histidyl-tRNA synthetase. Mol Gen Genet 100:216–224

    Google Scholar 

  • Nass G, Neidhardt FC (1967) Regulation of formation of aminoacyl ribonucleic acid synthetases in Escherichia coli. Biochem Biophys Acta 134:347–359

    Google Scholar 

  • Neidhardt FC, Bloch PL, Pedersen S, Reeh S (1977) Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J Bacteriol 129:378–387

    Google Scholar 

  • Neidhardt FC, Bloch PL, Smith DF (1974) Culture medium for enterobacteria. J Bacteriol 119:736–747

    Google Scholar 

  • Neidhardt FC, Parker J, McKeever WG (1975) Function and regulation of aminoacyl-tRNA synthetases in prokaryotic and eukaryotic cells. Ann Rev Microbiol 29:215–250

    Google Scholar 

  • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007–4021

    Google Scholar 

  • O'Farrell PH (1978) The suppression of defective translation by ppGpp and its role in the stringent response. Cell 14:545–557

    Google Scholar 

  • Parker J, Fishman SE (1979) Mapping hisS, the structural gene for histidyltransfer ribonucleic acid synthetase, in Escherichia coli. J Bacteriol 138:264–267

    Google Scholar 

  • Parker J, Pollard JW, Friesen JD, Stanners CP (1978) Stuttering: highlevel mistranslation in animal and bacterial cells. Proc Natl Acad Sci USA 75:1091–1095

    Google Scholar 

  • Pedersen S, Bloch PL, Reeh S, Neidhardt FC (1978) Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates. Cell 14:179–190

    Google Scholar 

  • Plumbridge JA, Springer M (1980) Genes for the two subunits of phenylalanyl-tRNA synthetase of Escherichia coli are transcribed from the same promoter. J Mol Biol 144:595–600

    Google Scholar 

  • Putney SD, Melendez DL, Schimmel PR (1981) Cloning, partial sequencing, and in vitro transcription of the gene for alanine tRNA synthetase. J Biol Chem 256:205–211

    Google Scholar 

  • Roth JR, Ames BN (1966) Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase. J Mol Biol 22:325–334

    Google Scholar 

  • Schimmel PR, Söll D (1979) Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Ann Rev Biochem 48:601–648

    Google Scholar 

  • Singer CE, Smith CR, Cortese R, Ames BN (1972) Mutant tRNAHis ineffective in repression and lacking two pseudouridine modifications. Nature (London) New Biol 238:72–74

    Google Scholar 

  • Sutcliffe JG (1979) pBR322 restriction map derived from DNA sequence: accurate DNA size markers up to 4361 nucleotide pairs long. Nucl Acids Res 5:2721–2728

    Google Scholar 

  • Szentirmai A, Umbarger HE (1968) Isoleucine and valine metaboism of Escherichia coli: XIV Effect of Thiaisoleucine. J Bacteriol 95:1666–1671

    Google Scholar 

  • Szybalski EH, Szybalski W (1979) A comprehensive molecular map of bacteriophage lambda. Gene 7:217–270

    Google Scholar 

  • Tanaka T, Weisblum B (1975) Construction of a colicin El-R factor composite plasmid in vitro: means for amplification of deoxyribonucleuc acid. J Bacteriol 121:354–362

    Google Scholar 

  • Thompson LH, Lofgren DJ, Adair GM (1977) CHO cell mutants for arginyl-, asparagyl-, glutaminyl-, histidyl- and methionyltransfer RNA synthetases: identification and initial characterization. Cell 11:157–168

    Google Scholar 

  • Williams LS, Neidhardt FC (1969) Synthesis and inactivation of aminoacyl-transfer RNA synthetases during growth of Escherichia coli. J Mol Biol 43:529–550

    Google Scholar 

  • Wyche JH, Ely B, Cebula TA, Snead MC, Hartman PE (1974) Histidyltransfer ribonucleic acid synthetase in positive control of the histidine operon in Salmonella typhimurium. J Bacteriol 117:708–716

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Microbiology, Southern Illinois University, 62901, Carbondale, Illinois, USA

    Scott J. Eisenbeis & Jack Parker

Authors
  1. Scott J. Eisenbeis
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jack Parker
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Communicated by A. Böck

Rights and permissions

Reprints and permissions

About this article

Cite this article

Eisenbeis, S.J., Parker, J. Strains of Escherichia coli carrying the structural gene for histidyl-tRNA synthetase on a high copy-number plasmid. Molec. Gen. Genet. 183, 115–122 (1981). https://doi.org/10.1007/BF00270148

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00270148

Keywords

Search

Navigation