Home LiteratureArticle Details
PMID: 2345136 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

tRNA(Trp) translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon.

Journal of bacteriology ·Vol. 172 ·No. 6 ·1990-06-00 ·Pages 3100-7

Gollnick P, Yanofsky C

Abstract

Tryptophanase (tna) operon expression in Escherichia coli is induced by tryptophan. This response is mediated by features of a 319-base-pair leader region preceding the major structural genes of the operon. Translation of the coding region (tnaC) for a 24-amino-acid leader peptide is essential for induction. We have used site-directed mutagenesis to investigate the role of the single Trp codon, at position 12 in tnaC, in regulation of the operon. Codon 12 was changed to either a UAG or UGA stop codon or to a CGG arginine codon. Induction by tryptophan was eliminated by any of these changes. Studies with suppressor tRNAs indicated that tRNA(Trp) translation of codon 12 in tnaC is essential for induction of the operon. Reduction of tna expression by a miaA mutation supports a role for translation by tRNA(Trp) in regulation of the operon. Frameshift mutations and suppression that allows translation of tnaC to proceed beyond the normal stop codon result in constitutive tna operon expression. Deletion of a potential site for Rho factor utilization just beyond tnaC also results in partial constitutive expression. These studies suggest possible models for tryptophan induction of tna operon expression involving tRNA(Trp)-mediated frame shifting or readthrough at the tnaC stop codon.

MeSH Terms
Chromosome Deletion Codon Gene Expression Regulation, Bacterial Lyases/genetics Mutation Nucleic Acid Conformation Operon Protein Biosynthesis Protein Sorting Signals/genetics RNA, Messenger RNA, Transfer, Amino Acid-Specific/metabolism RNA, Transfer, Trp/metabolism Suppression, Genetic Tryptophan/pharmacology Tryptophanase/genetics
Chemicals
Codon Protein Sorting Signals RNA, Messenger RNA, Transfer, Amino Acid-Specific RNA, Transfer, Trp Tryptophan Lyases Tryptophanase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gollnick P
Department of Biological Sciences, Stanford University, California 94305-5020.
Yanofsky C
References (36)
36 references, click to expand
  1. A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction.
    Science. 1987 May 15;236(4803):813-6 PMID: 3576200
  2. Construction of two Escherichia coli amber suppressor genes: tRNAPheCUA and tRNACysCUA.
    Proc Natl Acad Sci U S A. 1986 Sep;83(17):6548-52 PMID: 3529087
  3. Improved single and multicopy lac-based cloning vectors for protein and operon fusions.
    Gene. 1987;53(1):85-96 PMID: 3596251
  4. Sequence elements essential for rho-dependent transcription termination at lambda tR1.
    J Biol Chem. 1987 Aug 15;262(23):11292-9 PMID: 3038914
  5. Molecular cloning of the Escherichia coli miaA gene involved in the formation of delta 2-isopentenyl adenosine in tRNA.
    J Bacteriol. 1988 Sep;170(9):4147-52 PMID: 3045085
  6. Novel mechanisms of translational control in Saccharomyces cerevisiae.
    Trends Genet. 1988 Jun;4(6):169-74 PMID: 3076299
  7. CATALYTIC PROPERTIES OF TRYPTOPHANASE, A MULTIFUNCTIONAL PYRIDOXAL PHOSPHATE ENZYME.
    Proc Natl Acad Sci U S A. 1964 Mar;51:382-9 PMID: 14171448
  8. FORMATION AND INTERRELATIONSHIPS OF TRYPTOPHANASE AND TRYPTOPHAN SYNTHETASES IN ESCHERICHIA COLI.
    J Bacteriol. 1965 Feb;89:355-64 PMID: 14255701
  9. Mechanism of tryptophanase induction in Escherichia coli.
    J Mol Biol. 1967 Aug 14;27(3):495-506 PMID: 4860581
  10. Catabolite repression of tryptophanase in Escherichia coli.
    J Bacteriol. 1971 Jan;105(1):303-12 PMID: 4322348
  11. Tryptophan transfer RNA as the UGA suppressor.
    J Mol Biol. 1971 Jun 14;58(2):439-58 PMID: 4933412
  12. Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia.
    Proc Natl Acad Sci U S A. 1972 May;69(5):1086-90 PMID: 4556453
  13. Mutational alterations of tryptophan-specific transfer RNA that generate translation suppressors of the UAA, UAG and UGA nonsense codons.
    J Mol Biol. 1974 Jun 25;86(2):233-43 PMID: 4606830
  14. 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):663-77 PMID: 330867
  15. DNA sequencing with chain-terminating inhibitors.
    Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 PMID: 271968
  16. Interaction of secreted nascent chains with surrounding membrane in Bacillus subtilis.
    Proc Natl Acad Sci U S A. 1978 Dec;75(12):5922-5 PMID: 104295
  17. The effect of an Escherichia coli regulatory mutation on transfer RNA structure.
    J Mol Biol. 1979 Nov 25;135(1):111-26 PMID: 93644
  18. Dual specificity of su+ 7 tRNA. Evidence for translational discrimination.
    J Mol Biol. 1980 Jun 5;139(4):705-20 PMID: 6997500
  19. Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12.
    J Bacteriol. 1981 Sep;147(3):787-96 PMID: 6268608
  20. Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography.
    J Biol Chem. 1982 Aug 25;257(16):9759-69 PMID: 6286632
  21. Location of the gene for the low-affinity tryptophan-specific permease of Escherichia coli.
    Biochem J. 1982 May 15;204(2):617-9 PMID: 7052072
  22. New M13 vectors for cloning.
    Methods Enzymol. 1983;101:20-78 PMID: 6310323
  23. Repression is relieved before attenuation in the trp operon of Escherichia coli as tryptophan starvation becomes increasingly severe.
    J Bacteriol. 1984 Jun;158(3):1018-24 PMID: 6233264
  24. Defined set of cloned termination suppressors: in vivo activity of isogenetic UAG, UAA, and UGA suppressor tRNAs.
    J Bacteriol. 1984 Jun;158(3):849-59 PMID: 6327642
  25. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain.
    J Biol Chem. 1984 Aug 10;259(15):9790-8 PMID: 6086650
  26. Nucleotide sequence of yeast gene CP A1 encoding the small subunit of arginine-pathway carbamoyl-phosphate synthetase. Homology of the deduced amino acid sequence to other glutamine amidotransferases.
    Eur J Biochem. 1985 Jan 15;146(2):371-81 PMID: 3881260
  27. Transcription termination factor rho mediates simultaneous release of RNA transcripts and DNA template from complexes with Escherichia coli RNA polymerase.
    J Biol Chem. 1985 May 10;260(9):5826-31 PMID: 3886662
  28. RNA sequence and secondary structure requirements for rho-dependent transcription termination.
    Nucleic Acids Res. 1985 May 24;13(10):3739-54 PMID: 2409526
  29. Interaction of rho factor with bacteriophage lambda cro gene transcripts.
    J Biol Chem. 1985 Aug 5;260(16):9412-8 PMID: 3160698
  30. Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12.
    J Bacteriol. 1985 Nov;164(2):731-40 PMID: 3902796
  31. Differential inhibition of tryptophan synthase and of tryptophanase by the two diastereoisomers of 2,3-dihydro-L-tryptophan. Implications for the stereochemistry of the reaction intermediates.
    J Biol Chem. 1985 Nov 25;260(27):14665-70 PMID: 3902836
  32. The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA.
    Nucleic Acids Res. 1985 Dec 20;13(24):8765-85 PMID: 3001650
  33. Rho-dependent transcription termination in the tryptophanase operon leader region of Escherichia coli K-12.
    J Bacteriol. 1986 Apr;166(1):217-23 PMID: 2420781
  34. Fusion glycoprotein of human parainfluenza virus type 3: nucleotide sequence of the gene, direct identification of the cleavage-activation site, and comparison with other paramyxoviruses.
    Virology. 1986 Jul 15;152(1):241-51 PMID: 3012869
  35. Role of leader peptide synthesis in tryptophanase operon expression in Escherichia coli K-12.
    J Bacteriol. 1986 Jul;167(1):383-6 PMID: 3522554
  36. The leader peptide of yeast gene CPA1 is essential for the translational repression of its expression.
    Cell. 1987 Jun 19;49(6):805-13 PMID: 3555844
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.172.6.3100-3107.1990
Published
1990-06-00
Pages
3100-7
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC209113
Subset
IM
Grants
NIGMS NIH HHS · GM 09738 · United States
External Links
PubMed source DOI: 10.1128/jb.172.6.3100-3107.1990 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2