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Escherichia coli K-12 substr. MG1655 Enzyme: tryptophan synthase, β subunit dimer



Gene: trpB Accession Numbers: EG11025 (EcoCyc), b1261, ECK1255

Synonyms: β subunit, TSase β2, B protein, β2 protein

Regulation Summary Diagram: ?

Component of: tryptophan synthase (summary available)

Subunit composition of tryptophan synthase, β subunit dimer = [TrpB]2
         tryptophan synthase, β subunit = TrpB

Summary:
The TrpB polypeptide functions as the β subunit of the tetrameric (α22) tryptophan synthase complex [Hathaway70]. The TrpB protein forms a homodimer (TSase β2) in which each subunit contains a molecule of the cofactor pyridoxal 5'-phosphate (PLP) covalently linked to the ε-amino group of a lysine residue via a Schiff base [Bartholmes76]. This complex catalyzes the synthesis of L-tryptophan from indole and L-serine, also termed the β reaction.

The β2 subunit possesses binding sites for L-serine and PLP and can catalyze a variety of reactions involving these compounds [Tanizawa83].

The apo-β2 subunit has been used as a model system to study the mechanism of folding of protein oligomers [Planchenault96].

The crystal structure of the holo-tryptophan synthase β-subunit from Escherichia coli has been determined (see links to PDB: 2DH5, 2DH6), but a paper has not yet been published.

Gene Citations: [Yanofsky81, Yanofsky66, Imamoto65, Imamoto66]

Locations: cytosol

Map Position: [1,315,246 <- 1,316,439] (28.35 centisomes)
Length: 1194 bp / 397 aa

Molecular Weight of Polypeptide: 42.983 kD (from nucleotide sequence), 44.0 kD (experimental) [Gschwind79 ]

Molecular Weight of Multimer: 89.0 kD (experimental) [Adachi74]

pI: 6.04

Unification Links: ASAP:ABE-0004234 , CGSC:73 , EchoBASE:EB1018 , EcoGene:EG11025 , EcoliWiki:b1261 , Mint:MINT-7711989 , ModBase:P0A879 , OU-Microarray:b1261 , PortEco:trpB , PR:PRO_000024118 , Pride:P0A879 , Protein Model Portal:P0A879 , RefSeq:NP_415777 , RegulonDB:EG11025 , SMR:P0A879 , String:511145.b1261 , Swiss-Model:P0A879 , UniProt:P0A879

Relationship Links: InterPro:IN-FAMILY:IPR001926 , InterPro:IN-FAMILY:IPR006653 , InterPro:IN-FAMILY:IPR006654 , InterPro:IN-FAMILY:IPR023026 , Panther:IN-FAMILY:PTHR10314:SF3 , PDB:Structure:2DH5 , PDB:Structure:2DH6 , Pfam:IN-FAMILY:PF00291 , Prosite:IN-FAMILY:PS00168

In Paralogous Gene Group: 362 (8 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0000162 - tryptophan biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA06, GOA01, Zhao93]
GO:0009073 - aromatic amino acid family biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11, Zhao93]
GO:0006568 - tryptophan metabolic process Inferred by computational analysis [GOA01]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004834 - tryptophan synthase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Kaufmann91]
GO:0030170 - pyridoxal phosphate binding Inferred from experiment [Higgins78]
GO:0042802 - identical protein binding Inferred from experiment [Nishio10]
GO:0042803 - protein homodimerization activity Inferred from experiment [Hathaway70]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Murphy69]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, LopezCampistrou05]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids tryptophan

Essentiality data for trpB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 3]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
No [Feist07, Comment 4]

Credits:
Last-Curated ? 12-Feb-2010 by Fulcher C , SRI International


Enzymatic reaction of: tryptophan synthase

EC Number: 4.2.1.122

indole + L-serine <=> L-tryptophan + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown. [Kirschner91]

In Pathways: superpathway of chorismate metabolism , superpathway of phenylalanine, tyrosine, and tryptophan biosynthesis , tryptophan biosynthesis

Summary:
In this reaction indole condenses with L-serine to produce L-tryptophan. The ability of the isolated, purified holo-β2-subunit of tryptophan synthase (containing two molecules of pyridoxal 5'-phosphate bound per dimer) to catalyze this reaction was shown in experiments that compared the activities of native holo-β2-subunit and holo-β2-subunit proteolytically nicked at E-296 [Kaufmann91].

This β subunit-catalyzed partial reaction is considered to be practically irreversible (in [Lane91]).

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate [Kaufmann91]

T(opt): 40 °C [Bang83, BRENDA14, Zhao11b]

pH(opt): 8 [BRENDA14, Zhao11b]


Subunit of: tryptophan synthase

Subunit composition of tryptophan synthase = [TrpA]2[(TrpB)2]
         tryptophan synthase, α subunit = TrpA (extended summary available)
         tryptophan synthase, β subunit dimer = (TrpB)2 (extended summary available)
                 tryptophan synthase, β subunit = TrpB

Summary:
The physiologically active form of tryptophan synthase is a tetrameric α22 complex consisting of two α subunits (the protein product of the trpA gene) and a dimer of two β subunits (the protein product of the trpB gene). This complex catalyzes the last two steps in the biosynthesis of tryptophan [Lane91].

Although the α22 complex from Escherichia coli has been well studied, the purified α22 complex from Salmonella enterica subsp. enterica serovar Typhimurium (Salmonella typhimurium) provided crystals suitable for X-ray crystallography. Thus, the complex from this species has been studied in greater detail (reviewed in [Miles01, Dunn08]).

Molecular Weight: 146.5 kD (experimental) [Adachi74]

Credits:
Last-Curated ? 12-Feb-2010 by Fulcher C , SRI International


Enzymatic reaction of: tryptophan synthase

Synonyms: tryptophan desmolase, tryptophan synthetase

EC Number: 4.2.1.20

(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine <=> L-tryptophan + D-glyceraldehyde 3-phosphate + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown. [Kirschner91]

In Pathways: superpathway of chorismate metabolism , superpathway of phenylalanine, tyrosine, and tryptophan biosynthesis , tryptophan biosynthesis

Summary:
The overall tryptophan synthase reaction consists of a sequence of two partial reactions. The α subunit of the complex carries out the aldol cleavage of indole-3-glycerol phosphate to indole + glyceraldehyde-3-phosphate. The β subunit is responsible for the synthesis of L-tryptophan from indole + L-serine. The α22 complex, which alone catalyzes the overall reaction, proceeds at two independent α/β sites via catalysis of the α reaction on the α subunit component, channeling the product (indole) to the pyridoxal 5'-phosphate site on the β component, where, in the presence of L-serine, it is converted to tryptophan [Lane83, Dunn90] and reviewed in [Miles99]. Indole does not appear in solution and is not a free intermediate [Crawford58]. There is apparent subunit communication mediated by transduced conformational changes between the subunits, whereby the rates of the α and β reactions are strongly enhanced by, respectively, the β and α subunits [Lim91a, Kirschner91].

The partial reaction catalyzed by the α subunit is reversible [Yutani87], whereas the partial reaction catalyzed by the β subunit and the overall reaction catalyzed by the α22 complex are considered to be practically irreversible (in [Kirschner91]).

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate [Miles77]

Cofactor Binding Comment: Pyridoxal phosphate derivatives are much more strongly bound to the complex than to the beta subunit. This finding indicates that strong binding forces, in addition to the Schiff base linkage, exist in the complex, but not in the beta subunit. When this bond is broken during the formation of a derivative, the derivative is only weakly bound to the beta subunit, but is stongly bound to the complex by additional forces.[Miles77]

T(opt): 40 °C [Bang83, BRENDA14, Zhao11b]

pH(opt): 8 [BRENDA14, Zhao11b]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Higgins80, Link97, UniProt11]
UniProt: Removed.
Chain 2 -> 397
[UniProt09]
UniProt: Tryptophan synthase beta chain;
Active-Site 62
[Higgins80, UniProt11]
UniProt: Nucleophile.
Sequence-Conflict 78
[Higgins80, UniProt10a]
Alternate sequence: E → K; UniProt: (in Ref. 7; AA sequence);
Active-Site 86
[UniProt10]
UniProt: Proton donor; Non-Experimental Qualifier: probable;
N6-pyridoxal-phosphate-Lys-Modification 87
[UniProt11a]
UniProt: N6-(pyridoxal phosphate)lysine; Non-Experimental Qualifier: by similarity.
Extrinsic-Sequence-Variant 281
[UniProt10a]
Alternate sequence: G → R; UniProt: (in mutant TRPB8);
Sequence-Conflict 365
[Cotton72, UniProt11]
Alternate sequence: N → Z; UniProt: (in Ref. 10; AA sequence).
Sequence-Conflict 368 -> 369
[Cotton72, UniProt11]
Alternate sequence: KE → BK; UniProt: (in Ref. 10; AA sequence).


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1261 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11025; confirmed by SwissProt match.


References

Adachi74: Adachi O, Kohn LD, Miles EW (1974). "Crystalline alpha2 beta2 complexes of tryptophan synthetase of Escherichia coli. A comparison between the native complex and the reconstituted complex." J Biol Chem 249(24);7756-63. PMID: 4609974

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bang83: Bang WG, Lang S, Sahm H, Wagner F (1983). "Production L-tryptophan by Escherichia coli cells." Biotechnol Bioeng 25(4);999-1011. PMID: 18548715

Bartholmes76: Bartholmes P, Kirschner K, Gschwind HP (1976). "Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli." Biochemistry 15(21);4712-7. PMID: 788781

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Cotton72: Cotton RG, Crawford IP (1972). "Tryptophan synthetase B 2 subunit. Application of genetic analysis to the study of primary structure." J Biol Chem 247(6);1883-91. PMID: 4552018

Crawford58: Crawford IP, Yanofsky C (1958). "On the separation of the tryptophan synthetase of Escherichia coli into two protein components." Proc Natl Acad Sci U S A 44(12);1161-70. PMID: 16590328

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dunn08: Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I (2008). "Tryptophan synthase: the workings of a channeling nanomachine." Trends Biochem Sci 33(6);254-64. PMID: 18486479

Dunn90: Dunn MF, Aguilar V, Brzovic P, Drewe WF, Houben KF, Leja CA, Roy M (1990). "The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel." Biochemistry 29(37);8598-607. PMID: 2271543

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gschwind79: Gschwind HP, Gschwind U, Paul CH, Kirschner K (1979). "Affinity chromatography of tryptophan synthase from Escherichia coli. Systematic studies with immobilized tryptophanol phosphate." Eur J Biochem 96(2);403-16. PMID: 378665

Hathaway70: Hathaway GM, Crawford IP (1970). "Studies on the association of beta-chain monomers of Escherichia coli tryptophan synthetase." Biochemistry 9(8);1801-8. PMID: 4909082

Higgins78: Higgins W, Miles EW (1978). "Affinity labeling of the pyridoxal phosphate binding site of the beta2 subunit of Escherichia coli tryptophan synthase." J Biol Chem 253(13);4648-52. PMID: 350880

Higgins80: Higgins W, Miles EW, Fairwell T (1980). "Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli." J Biol Chem 255(2);512-7. PMID: 6985892

Imamoto65: Imamoto F, Morikawa N, Sato K (1965). "On the transcription of the tryptophan operon in Escherichia coli. 3. Multicistronic messenger RNA and polarity for transcription." J Mol Biol 13(1);169-82. PMID: 5323613

Imamoto66: Imamoto F, Ito J, Yanofsky C (1966). "Polarity in the tryptophan operon of E. coli." Cold Spring Harb Symp Quant Biol 31;235-49. PMID: 4866380

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kaufmann91: Kaufmann M, Schwarz T, Jaenicke R, Schnackerz KD, Meyer HE, Bartholmes P (1991). "Limited proteolysis of the beta 2-dimer of tryptophan synthase yields an enzymatically active derivative that binds alpha-subunits." Biochemistry 30(17);4173-9. PMID: 2021608

Kirschner91: Kirschner K, Lane AN, Strasser AW (1991). "Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex." Biochemistry 1991;30(2);472-8. PMID: 1899027

Lane83: Lane AN, Kirschner K (1983). "The catalytic mechanism of tryptophan synthase from Escherichia coli. Kinetics of the reaction of indole with the enzyme--L-serine complexes." Eur J Biochem 129(3);571-82. PMID: 6402362

Lane91: Lane AN, Kirschner K (1991). "Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli." Biochemistry 30(2);479-84. PMID: 1899028

Lim91a: Lim WK, Shin HJ, Milton DL, Hardman JK (1991). "Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits." J Bacteriol 1991;173(6);1886-93. PMID: 2001993

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Miles01: Miles EW (2001). "Tryptophan synthase: a multienzyme complex with an intramolecular tunnel." Chem Rec 1(2);140-51. PMID: 11893063

Miles77: Miles EW, Moriguchi M (1977). "Tryptophan synthase of Escherichia coli. Removal of pyridoxal 5'-phosphate and separation of the alpha and beta2 subunits." J Biol Chem 1977;252(19);6594-9. PMID: 330534

Miles99: Miles EW, Rhee S, Davies DR (1999). "The molecular basis of substrate channeling." J Biol Chem 274(18);12193-6. PMID: 10212181

Murphy69: Murphy TM, Mills SE (1969). "Immunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae." J Bacteriol 97(3);1310-20. PMID: 4887511

Nishio10: Nishio K, Ogasahara K, Morimoto Y, Tsukihara T, Lee SJ, Yutani K (2010). "Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5'-phosphate binding." FEBS J 277(9);2157-70. PMID: 20370823

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

Planchenault96: Planchenault T, Navon A, Schulze AJ, Goldberg ME (1996). "Transient non-native interactions in early folding intermediates do not influence the folding kinetics of Escherichia coli tryptophan synthase beta 2 subunits." Eur J Biochem 240(3);615-21. PMID: 8856062

Tanizawa83: Tanizawa K, Miles EW (1983). "L-serine binds to arginine-148 of the beta 2 subunit of Escherichia coli tryptophan synthase." Biochemistry 22(15);3594-603. PMID: 6412746

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Yanofsky66: Yanofsky C, Ito J (1966). "Nonsense codons and polarity in the tryptophan operon." J Mol Biol 21(2);313-34. PMID: 5339605

Yanofsky81: Yanofsky C, Platt T, Crawford IP, Nichols BP, Christie GE, Horowitz H, VanCleemput M, Wu AM (1981). "The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Nucleic Acids Res 1981;9(24);6647-68. PMID: 7038627

Yutani87: Yutani K, Ogasahara K, Tsujita T, Kanemoto K, Matsumoto M, Tanaka S, Miyashita T, Matsushiro A, Sugino Y, Miles EW (1987). "Tryptophan synthase alpha subunit glutamic acid 49 is essential for activity. Studies with 19 mutants at position 49." J Biol Chem 262(28);13429-33. PMID: 2888759

Zhao11b: Zhao G, Liu J, Dong K, Zhang F, Zhang H, Liu Q, Jiao Q (2011). "Enzymatic synthesis of L-tryptophan from hair acid hydrolysis industries wastewater with tryptophan synthase." Bioresour Technol 102(3);3554-7. PMID: 20884203

Zhao93: Zhao GP, Somerville RL (1993). "A single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product." J Biol Chem 268(20);14921-31. PMID: 8325869

Other References Related to Gene Regulation

Bass87: Bass S, Sugiono P, Arvidson DN, Gunsalus RP, Youderian P (1987). "DNA specificity determinants of Escherichia coli tryptophan repressor binding." Genes Dev 1(6);565-72. PMID: 3315854

Bertrand76a: Bertrand K, Squires C, Yanofsky C (1976). "Transcription termination in vivo in the leader region of the tryptophan operon of Escherichia coli." J Mol Biol 103(2);319-37. PMID: 781269

Bertrand76b: Bertrand K, Yanofsky C (1976). "Regulation of transcription termination in the leader region of the tryptophan operon of Escherichia coli involves tryptophan or its metabolic product." J Mol Biol 103(2);339-49. PMID: 781270

Bertrand77: Bertrand K, Korn LJ, Lee F, Yanofsky C (1977). "The attenuator of the tryptophan operon of Escherichia coli. Heterogeneous 3'-OH termini in vivo and deletion mapping of functions." J Mol Biol 117(1);227-47. PMID: 340702

Fisher85: Fisher RF, Das A, Kolter R, Winkler ME, Yanofsky C (1985). "Analysis of the requirements for transcription pausing in the tryptophan operon." J Mol Biol 182(3);397-409. PMID: 2409288

Grandori98: Grandori R, Khalifah P, Boice JA, Fairman R, Giovanielli K, Carey J (1998). "Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins." J Biol Chem 273(33);20960-6. PMID: 9694845

Gunsalus80: Gunsalus RP, Yanofsky C (1980). "Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor." Proc Natl Acad Sci U S A 1980;77(12);7117-21. PMID: 7012834

Hiraga73: Hiraga S, Yanofsky C (1973). "Inhibition of the progress of transcription on the tryptophan operon of Escherichia coli." J Mol Biol 79(2);339-49. PMID: 4586412

Horowitz82: Horowitz H, Platt T (1982). "Identification of trp-p2, an internal promoter in the tryptophan operon of Escherichia coli." J Mol Biol 1982;156(2);257-67. PMID: 7045383

Horowitz83: Horowitz H, Platt T (1983). "Initiation in vivo at the internal trp p2 promoter of Escherichia coli." J Biol Chem 1983;258(13);7890-3. PMID: 6305961

Imamoto68: Imamoto F (1968). "On the initiation of transcription of the tryptophan operon in Escherichia coli." Proc Natl Acad Sci U S A 60(1);305-12. PMID: 4872441

Jackson73: Jackson EN, Yanofsky C (1973). "Thr region between the operator and first structural gene of the tryptophan operon of Escherichia coli may have a regulatory function." J Mol Biol 76(1);89-101. PMID: 4578102

Jeeves99: Jeeves M, Evans PD, Parslow RA, Jaseja M, Hyde EI (1999). "Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences." Eur J Biochem 1999;265(3);919-28. PMID: 10518785

Klig88: Klig LS, Carey J, Yanofsky C (1988). "trp repressor interactions with the trp aroH and trpR operators. Comparison of repressor binding in vitro and repression in vivo." J Mol Biol 1988;202(4);769-77. PMID: 3050131

Kumamoto87: Kumamoto AA, Miller WG, Gunsalus RP (1987). "Escherichia coli tryptophan repressor binds multiple sites within the aroH and trp operators." Genes Dev 1(6);556-64. PMID: 3315853

Landick85: Landick R, Carey J, Yanofsky C (1985). "Translation activates the paused transcription complex and restores transcription of the trp operon leader region." Proc Natl Acad Sci U S A 82(14);4663-7. PMID: 2991886

Oxender79: Oxender DL, Zurawski G, Yanofsky C (1979). "Attenuation in the Escherichia coli tryptophan operon: role of RNA secondary structure involving the tryptophan codon region." Proc Natl Acad Sci U S A 76(11);5524-8. PMID: 118451

Platt76: Platt T, Squires C, Yanofsky C (1976). "Ribosome-protected regions in the leader-trpE sequence of Escherichia coli tryptophan operon messenger RNA." J Mol Biol 103(2);411-20. PMID: 781274

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Squires76: Squires C, Lee F, Bertrand K, Squires CL, Bronson MJ, Yanofsky C (1976). "Nucleotide sequence of the 5' end of tryptophan messenger RNA of Escherichia coli." J Mol Biol 103(2);351-81. PMID: 781271

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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