tnaA

Summary

Gene Symbol: tnaA
Description: tryptophanase/L-cysteine desulfhydrase, PLP-dependent
Alias: ECK3701, JW3686, ind
Species: Escherichia coli str. K-12 substr. MG1655
Products:     tnaA

Top Publications

  1. Kogan A, Gdalevsky G, Cohen Luria R, Parola A, Goldgur Y. Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase. Acta Crystallogr D Biol Crystallogr. 2004;60:2073-5 pubmed
    ..9 A. Data sets of wild-type crystals soaked with L-tryptophan or pyridoxal phosphate were collected, as well as of Y74F mutant soaked with both. ..
  2. Phillips R, Demidkina T, Faleev N. Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase. Biochim Biophys Acta. 2003;1647:167-72 pubmed
    ..Thus, additional residues remote from the active site may be needed for substrate specificity. Both Trpase and TPL may react by a rare S(E)2-type mechanism. ..
  3. Ku S, Yip P, Howell P. Structure of Escherichia coli tryptophanase. Acta Crystallogr D Biol Crystallogr. 2006;62:814-23 pubmed
  4. Burns R, DeMoss R. Properties of tryptophanase from Escherichia coli. Biochim Biophys Acta. 1962;65:233-44 pubmed
  5. Erez T, Phillips R, Parola A. Pyridoxal phosphate binding to wild type, W330F, and C298S mutants of Escherichia coli apotryptophanase: unraveling the cold inactivation. FEBS Lett. 1998;433:279-82 pubmed
    ..It is suggested that during the cold inactivation process a conformational change precedes the aldimine bond cleavage. For the W330F apotryptophanase, another conformational change occurs subsequent to the aldimine bond cleavage. ..
  6. Phillips R, Holtermann G. Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase. Biochemistry. 2005;44:14289-97 pubmed
  7. Phillips R, Gollnick P. Evidence that cysteine 298 is in the active site of tryptophan indole-lyase. J Biol Chem. 1989;264:10627-32 pubmed
    ..However, these data suggest that Cys-298 is located within or very near the active site of the enzyme and is the reactive cysteine residue previously observed by others. ..
  8. Raibaud O, Goldberg M. The tryptophanase from Escherichia coli K-12. II. Comparison of the thermal stabilities of apo-, holo-, and hybrid enzymes. J Biol Chem. 1973;248:3451-5 pubmed
  9. Isaacs H, Chao D, Yanofsky C, Saier M. Mechanism of catabolite repression of tryptophanase synthesis in Escherichia coli. Microbiology. 1994;140 ( Pt 8):2125-34 pubmed
    ..Both mechanisms are attributable to depressed rates of cyclic AMP synthesis. No evidence for a cyclic-AMP-independent mechanism of catabolite repression was obtained. ..

More Information

Publications62

  1. Otsuka Y, Koga M, Iwamoto A, Yonesaki T. A role of RnlA in the RNase LS activity from Escherichia coli. Genes Genet Syst. 2007;82:291-9 pubmed
    ..Among these, triose phosphate isomerase exhibited a remarkable affinity to RnlA. These results suggest that RnlA plays a central role in RNase LS activity and that its activity is regulated by multiple components...
  2. Zheng C, Yang L, Hoopmann M, Eng J, Tang X, Weisbrod C, et al. Cross-linking measurements of in vivo protein complex topologies. Mol Cell Proteomics. 2011;10:M110.006841 pubmed publisher
    ..Furthermore, our unbiased data provide novel in vivo topological information that can impact understanding of biological function, even for cases where high resolution structures are not yet available. ..
  3. Kogan A, Gdalevsky G, Cohen Luria R, Goldgur Y, Phillips R, Parola A, et al. Conformational changes and loose packing promote E. coli Tryptophanase cold lability. BMC Struct Biol. 2009;9:65 pubmed publisher
    ..The hydrophobic interactions along the non catalytic interface overshadow the effect of point mutations and may account for the differences in the dissociation of E. coli Trpase to dimers and P. vulgaris Trpase to monomers. ..
  4. Konan K, Yanofsky C. Rho-dependent transcription termination in the tna operon of Escherichia coli: roles of the boxA sequence and the rut site. J Bacteriol. 2000;182:3981-8 pubmed
    ..Studies with a lacZ reporter construct lacking the tnaC-tnaA spacer region suggest that, in the presence of excess tryptophan, the TnaC leader peptide acts in cis on the ..
  5. Martino P, Fursy R, Bret L, Sundararaju B, Phillips R. Indole can act as an extracellular signal to regulate biofilm formation of Escherichia coli and other indole-producing bacteria. Can J Microbiol. 2003;49:443-9 pubmed
    ..coli 3714 (S17-1 tnaA::Tn5) in LB medium...
  6. Michel Reydellet N, Calhoun K, Swartz J. Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome. Metab Eng. 2004;6:197-203 pubmed
    ..Cysteine, however, continues to be degraded. Cell-free protein synthesis with the modified cell extract produces increased yields of the cysteine-free protein Outer Membrane Protein T (OmpT). ..
  7. Kagamiyama H, Matsubara H, Snell E. The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides. J Biol Chem. 1972;247:1576-86 pubmed
  8. Li G, Young K. A cAMP-independent carbohydrate-driven mechanism inhibits tnaA expression and TnaA enzyme activity in Escherichia coli. Microbiology. 2014;160:2079-88 pubmed publisher
    ..the contributions of TolC and CpdA by measuring the expression of cAMP-regulated genes that encode tryptophanase (TnaA) and ?-galactosidase...
  9. Zhang Y, Hong G. Evidences of Hfq associates with tryptophanase and affects extracellular indole levels. Acta Biochim Biophys Sin (Shanghai). 2009;41:709-17 pubmed
    ..Indole was produced by tryptophanase, the gene product of tnaA, which catalyzed tryptophan into indole, ammonia and pyruvate. Further studies showed that at cell density of 0...
  10. Li G, Young K. A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active site. BMC Microbiol. 2015;15:14 pubmed publisher
    The Escherichia coli enzyme tryptophanase (TnaA) converts tryptophan to indole, which triggers physiological changes and regulates interactions between bacteria and their mammalian hosts...
  11. Kogan A, Raznov L, Gdalevsky G, Cohen Luria R, Almog O, Parola A, et al. Structures of Escherichia coli tryptophanase in holo and 'semi-holo' forms. Acta Crystallogr F Struct Biol Commun. 2015;71:286-90 pubmed publisher
    ..Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase. ..
  12. Mizobata T, Akiyama Y, Ito K, Yumoto N, Kawata Y. Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP. J Biol Chem. 1992;267:17773-9 pubmed
    ..The conformation formed in the presence of ADP was distinct from the conformation formed in the presence of ATP, as shown by the selective dissociation of various folding proteins from the two conformations. ..
  13. Deeley M, Yanofsky C. Transcription initiation at the tryptophanase promoter of Escherichia coli K-12. J Bacteriol. 1982;151:942-51 pubmed
    Restriction fragments containing the region preceding the tryptophanase structural gene, tnaA, were used as templates for in vitro transcription experiments...
  14. Grudniak A, Nowicka Sans B, Maciag M, Wolska K. Influence of Escherichia coli DnaK and DnaJ molecular chaperones on tryptophanase (TnaA) amount and GreA, GreB stability. Folia Microbiol (Praha). 2004;49:507-12 pubmed
    ..The half-life of GreA and GreB proteins (being activators of transcription elongation of the tna operon) are diminished in both mutants suggesting the involvement of DnaK and DnaJ in the stability of these proteins. ..
  15. Kuczynska Wisnik D, Matuszewska E, Laskowska E. Escherichia coli heat-shock proteins IbpA and IbpB affect biofilm formation by influencing the level of extracellular indole. Microbiology. 2010;156:148-57 pubmed publisher
    ..We demonstrated that the formation of biofilm by the ibpAB mutant was delayed due to the increase in the extracellular concentration of indole, which is known to play the role of a signal molecule, inhibiting biofilm growth. ..
  16. Allen M, White G, Morby A. The response of Escherichia coli to exposure to the biocide polyhexamethylene biguanide. Microbiology. 2006;152:989-1000 pubmed
  17. Collet A, Vilain S, Cosette P, Junter G, Jouenne T, Phillips R, et al. Protein expression in Escherichia coli S17-1 biofilms: impact of indole. Antonie Van Leeuwenhoek. 2007;91:71-85 pubmed
    ..coli S17-1 wild-type and 3714 (S17-1 tnaA::Tn5) tryptophanase-negative mutant cells (which don't produce indole) grown as suspensions or biofilms in the ..
  18. Wang D, Ding X, Rather P. Indole can act as an extracellular signal in Escherichia coli. J Bacteriol. 2001;183:4210-6 pubmed
    ..Conditioned medium prepared from a tnaA (tryptophanase) mutant, deficient in indole production, supported 26 to 41% lower activation of the gabT and astD ..
  19. Phillips R. Reaction of indole and analogues with amino acid complexes of Escherichia coli tryptophan indole-lyase: detection of a new reaction intermediate by rapid-scanning stopped-flow spectrophotometry. Biochemistry. 1991;30:5927-34 pubmed
    ..This new intermediate is formed faster than catalytic turnover (kcat = 6.8 s-1) and may be an alpha-aminoacrylate intermediate bound as a gem-diamine. ..
  20. Gish K, Yanofsky C. Inhibition of expression of the tryptophanase operon in Escherichia coli by extrachromosomal copies of the tna leader region. J Bacteriol. 1993;175:3380-7 pubmed
    ..translation of a 24-residue coding region, tnaC, located in the 319-nucleotide transcribed leader region preceding tnaA, the structural gene for tryptophanase...
  21. Li G, Young K. Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol Microbiol. 2012;84:276-95 pubmed publisher
    ..GFP-fused derivatives of four candidates (Aer, YqjD, TnaA and GroES) formed polar foci that were distinct from inclusion bodies...
  22. Deeley M, Yanofsky C. Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12. J Bacteriol. 1981;147:787-96 pubmed
    The tryptophanase structural gene, tnaA, of Escherichia coli K-12 was cloned and sequenced...
  23. Watanabe T, Snell E. Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia. Proc Natl Acad Sci U S A. 1972;69:1086-90 pubmed
  24. Awano N, Wada M, Mori H, Nakamori S, Takagi H. Identification and functional analysis of Escherichia coli cysteine desulfhydrases. Appl Environ Microbiol. 2005;71:4149-52 pubmed
    ..The gene disruption for each protein was significantly effective for overproduction of L-cysteine and L-cystine. Growth phenotype and transcriptional analyses suggest that tryptophanase contributes primarily to L-cysteine degradation. ..
  25. Green K, Qasim N, Gdaelvsky G, Kogan A, Goldgur Y, Parola A, et al. A structural view of the dissociation of Escherichia coli tryptophanase. Acta Crystallogr D Biol Crystallogr. 2015;71:2364-71 pubmed publisher
    ..Thus, the results indicate that dissociation of E. coli Trpase into dimers occurs along the molecular Q axis. ..
  26. Yudkin M. Unstable mutations that relieve catabolite repression of tryptophanase synthesis by Escherichia coli. J Bacteriol. 1977;130:57-61 pubmed
    ..Each of the mutants segregated variants of the parental type. The results of genetic analysis appear to be consistent with the mutants arose by duplication of the tryptophanase gene. ..
  27. Kwon Y, Weiss B. Production of 3-nitrosoindole derivatives by Escherichia coli during anaerobic growth. J Bacteriol. 2009;191:5369-76 pubmed publisher
    ..The reaction requires functional genes for trytophanase (tnaA), a tryptophan permease (tnaB), and a nitrate reductase (narG), as well as a natural drop in the pH of the culture...
  28. Stewart V, Yanofsky C. Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12. J Bacteriol. 1985;164:731-40 pubmed
    Tryptophanase, encoded by the gene tnaA, is a catabolic enzyme distinct from the enzymes of tryptophan biosynthesis. Tryptophanase synthesis is induced by tryptophan and is subject to catabolite repression...
  29. Gartner T, Riley M. GENETIC ANALYSIS OF TRYPTOPHANASE MUTANTS OF ESCHERICHIA COLI. J Bacteriol. 1965;89:319-25 pubmed
    ..Another regulation gene, R(2)tna, confers constitutivity at 13 C and does not map at the same locus as the R(2)tna gene. ..
  30. Edwards R, Yudkin M. Location of the gene for the low-affinity tryptophan-specific permease of Escherichia coli. Biochem J. 1982;204:617-9 pubmed
    ..A mutant carrying a deletion from bgl through tnaA showed negligible L-tryptophan uptake, in contrast to a strain possessing an intact tna region or to strains ..
  31. Gong F, Yanofsky C. Rho's role in transcription attenuation in the tna operon of E. coli. Methods Enzymol. 2003;371:383-91 pubmed
  32. Tokushige M, Tsujimoto N, Oda T, Honda T, Yumoto N, Ito S, et al. Role of cysteine residues in tryptophanase for monovalent cation-induced activation. Biochimie. 1989;71:711-20 pubmed
    ..The above results are compatible with the possibility that Cys-298 is involved in the formation of "monovalent cation binding site" in the holoenzyme. ..
  33. Gollnick P, Yanofsky C. tRNA(Trp) translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon. J Bacteriol. 1990;172:3100-7 pubmed
    ..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. ..
  34. Yamada S, Awano N, Inubushi K, Maeda E, Nakamori S, Nishino K, et al. Effect of drug transporter genes on cysteine export and overproduction in Escherichia coli. Appl Environ Microbiol. 2006;72:4735-42 pubmed
    ..of the acrD, acrEF, bcr, cusA, emrAB, emrKY, ybjYZ, and yojIH genes reversed the growth inhibition of tnaA (the major CD gene)-disrupted E. coli cells by L-cysteine...
  35. Cruz Vera L, Yanofsky C. Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of Tna operon expression. J Bacteriol. 2008;190:4791-7 pubmed publisher
  36. Blankenhorn D, Phillips J, Slonczewski J. Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis. J Bacteriol. 1999;181:2209-16 pubmed
    ..At pH 9, tryptophan deaminase (TnaA) was induced to a high level, becoming one of the most abundant proteins observed...
  37. Chant E, Summers D. Indole signalling contributes to the stable maintenance of Escherichia coli multicopy plasmids. Mol Microbiol. 2007;63:35-43 pubmed
    ..This is an novel role for this molecule which previously has been implicated in quorum sensing-like processes at high cell density. ..
  38. Li G, Young K. Indole production by the tryptophanase TnaA in Escherichia coli is determined by the amount of exogenous tryptophan. Microbiology. 2013;159:402-10 pubmed publisher
    ..In Escherichia coli, the enzyme tryptophanase (TnaA) produces indole from tryptophan, but it is not clear what determines how much indole E...
  39. Snell E. Tryptophanase: structure, catalytic activities, and mechanism of action. Adv Enzymol Relat Areas Mol Biol. 1975;42:287-333 pubmed
  40. Rieger R, Zaika E, Xie W, Johnson F, Grollman A, Iden C, et al. Proteomic approach to identification of proteins reactive for abasic sites in DNA. Mol Cell Proteomics. 2006;5:858-67 pubmed
    ..We report identification of seven proteins from Escherichia coli (AroF, DnaK, MutM, PolA, TnaA, TufA, and UvrA) and two proteins from bakers' yeast (ARC1 and Ygl245wp) reactive for AP sites in this system.
  41. Ng H, Gartner T. Selection of mutants of Escherichia coli constitutive for tryptophanase. J Bacteriol. 1963;85:245-6 pubmed
  42. Awano N, Wada M, Kohdoh A, Oikawa T, Takagi H, Nakamori S. Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli. Appl Microbiol Biotechnol. 2003;62:239-43 pubmed
    ..with gene-disrupted mutants showed that CD activity resulted from two enzymes: tryptophanase (TNase) encoded by tnaA and cystathionine beta-lyase (CBL) encoded by metC...
  43. Rompf A, Schmid R, Jahn D. Changes in protein synthesis as a consequence of heme depletion in Escherichia coli. Curr Microbiol. 1998;37:226-30 pubmed
    ..All induced genes are under the control of the catabolite repressor protein Crp. The observed changes in gene expression as a consequence of heme depletion are discussed. ..
  44. Stewart V, Landick R, Yanofsky C. Rho-dependent transcription termination in the tryptophanase operon leader region of Escherichia coli K-12. J Bacteriol. 1986;166:217-23 pubmed
    ..In vivo termination appeared to occur at the rho-dependent termination sites identified in vitro. Transcription pausing analyses correlated sites of pausing in tnaL with sites of rho-dependent termination. ..
  45. Miki T, Kimura M, Hiraga S, Nagata T, Yura T. Cloning and physical mapping of the dnaA region of the Escherichia coli chromosome. J Bacteriol. 1979;140:817-24 pubmed
    ..29 Md, containing the 3.5-Md dnaA substitution segment, from the lambda i21 dnaA-2 DNA, inserting it into the sole BamHI cleavage site on pBR322. ..
  46. Yanofsky C. RNA-based regulation of genes of tryptophan synthesis and degradation, in bacteria. RNA. 2007;13:1141-54 pubmed
    ..I will also describe the RNA-based mechanism used by E. coli in regulating expression of its operon responsible for tryptophan degradation, the tryptophanase operon. ..
  47. Kobayashi A, Hirakawa H, Hirata T, Nishino K, Yamaguchi A. Growth phase-dependent expression of drug exporters in Escherichia coli and its contribution to drug tolerance. J Bacteriol. 2006;188:5693-703 pubmed
    ..The induction level was decreased by tnaAB deletion, suggesting that indole sensing stimulates this process. ..
  48. Uc Mass A, Khodursky A, Brown L, Gottesman M. Overexpression of phage HK022 Nun protein is toxic for Escherichia coli. J Mol Biol. 2008;380:812-9 pubmed publisher
    ..Microarray and proteomic analyses show that Nun down-regulates crp and tnaA. Crp overexpression and high indole concentrations partially reverse Nun-mediated toxicity and restore lacZ ..
  49. Anyanful A, Dolan Livengood J, Lewis T, Sheth S, Dezalia M, Sherman M, et al. Paralysis and killing of Caenorhabditis elegans by enteropathogenic Escherichia coli requires the bacterial tryptophanase gene. Mol Microbiol. 2005;57:988-1007 pubmed
    ..Together, these data suggest that this C. elegans/EPEC system will be valuable in elucidating novel factors relevant to human disease that regulate virulence in the pathogen or susceptibility to infection in the host. ..
  50. Polissi A, De Laurentis W, Zangrossi S, Briani F, Longhi V, Pesole G, et al. Changes in Escherichia coli transcriptome during acclimatization at low temperature. Res Microbiol. 2003;154:573-80 pubmed
    ..Interestingly, we found that PNPase both negatively and positively modulated the transcript abundance of some of these genes, thus suggesting a complex role of PNPase in controlling cold adaptation. ..
  51. Gong F, Yanofsky C. Instruction of translating ribosome by nascent peptide. Science. 2002;297:1864-7 pubmed
    ..The location of tryptophan-12 of nascent TnaC in the peptide exit tunnel was crucial for induction. These results show that a nascent peptide sequence can influence translation continuation and termination within a translating ribosome. ..
  52. London J, Goldberg M. The tryptophanase from Escherichia coli K-12. I. Purification, physical properties, and quaternary structure. J Biol Chem. 1972;247:1566-70 pubmed
  53. Sarsero J, Wookey P, Gollnick P, Yanofsky C, Pittard A. A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli. J Bacteriol. 1991;173:3231-4 pubmed
    ..TnaB is a tryptophan-specific permease that is homologous to Mtr, a second tryptophan-specific permease, and to TyrP, a tyrosine-specific permease. Each member of this family appears to contain 11 membrane-spanning domains. ..