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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Polypeptide: phenylalanyl-tRNA synthetase β-chain



Gene: pheT Accession Numbers: EG10710 (EcoCyc), b1713, ECK1711

Regulation Summary Diagram: ?

Component of: phenylalanyl-tRNA synthetase (extended summary available)

Summary:
The β subunit of PheRS contains the Phe-tRNAPhe binding site [Lavrik82, Khodyreva85]. The editing site of the enzyme localizes to the B3/B4 domain of the β subunit [Roy04a]. Amino acid residues involved in the editing activity have been identified [Ling07]. The B2 OB-fold domain is not essential for catalytic activity, but may play a role as a secondary tRNA binding site in post-transfer editing [Roy06].

Isolated β subunits exist primarily as monomers [Bobkova91].

Citations: [Comer76, Russell71]

Gene Citations: [Fayat83, Wertheimer88, Springer85, Mechulam85, Mayaux84, Springer83, Mayaux85, Trudel84]

Locations: cytosol, membrane

Map Position: [1,793,581 <- 1,795,968] (38.66 centisomes)
Length: 2388 bp / 795 aa

Molecular Weight of Polypeptide: 87.378 kD (from nucleotide sequence), 98 kD (experimental) [Ducruix83 ]

Unification Links: ASAP:ABE-0005717 , CGSC:399 , DIP:DIP-6879N , EchoBASE:EB0704 , EcoGene:EG10710 , EcoliWiki:b1713 , Mint:MINT-1231494 , ModBase:P07395 , OU-Microarray:b1713 , PortEco:pheT , Pride:P07395 , Protein Model Portal:P07395 , RefSeq:NP_416228 , RegulonDB:EG10710 , SMR:P07395 , String:511145.b1713 , UniProt:P07395

Relationship Links: InterPro:IN-FAMILY:IPR002547 , InterPro:IN-FAMILY:IPR004532 , InterPro:IN-FAMILY:IPR005121 , InterPro:IN-FAMILY:IPR005146 , InterPro:IN-FAMILY:IPR005147 , InterPro:IN-FAMILY:IPR009061 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR020825 , PDB:Structure:3PCO , Pfam:IN-FAMILY:PF01588 , Pfam:IN-FAMILY:PF03147 , Pfam:IN-FAMILY:PF03483 , Pfam:IN-FAMILY:PF03484 , Prosite:IN-FAMILY:PS50886 , Prosite:IN-FAMILY:PS51447 , Prosite:IN-FAMILY:PS51483 , Smart:IN-FAMILY:SM00873 , Smart:IN-FAMILY:SM00874 , Smart:IN-FAMILY:SM00896

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006432 - phenylalanyl-tRNA aminoacylation Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Comer76]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11]
GO:0008033 - tRNA processing Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Lasserre06, Butland05]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Lasserre06]
GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06, GOA01]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0004812 - aminoacyl-tRNA ligase activity Inferred by computational analysis [UniProtGOA11]
GO:0004826 - phenylalanine-tRNA ligase activity Inferred by computational analysis [GOA06, GOA01a, GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0009328 - phenylalanine-tRNA ligase complex Inferred from experiment [Fayat74]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, GOA01]

MultiFun Terms: information transfer protein related amino acid -activation

Essentiality data for pheT knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Last-Curated ? 30-Jun-2014 by Keseler I , SRI International


Subunit of: phenylalanyl-tRNA synthetase

Subunit composition of phenylalanyl-tRNA synthetase = [PheS]2[PheT]2
         phenylalanyl-tRNA synthetase α-chain = PheS (summary available)
         phenylalanyl-tRNA synthetase β-chain = PheT (summary available)

Summary:
Phenylalanyl-tRNA synthetase (PheRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. The reaction is driven by ATP hydrolysis. PheRS belongs to the Class IIC aminoacyl tRNA synthetases [Eriani90, Cusack91, Perona12].

PheRS is a tetramer consisting of two α and two β subunits. Both subunits are required for catalytic activity [Fayat74, Ducruix83]. Two molecules of tRNAPhe bind to one PheRS complex [Dessen83], and both binding sites are active sites [Bartmann75, Hennecke76]. Binding is not dependent on Mg2+ [Krauss75]. A crystal structure of PheRS in a complex with phenylalanine and AMP has been solved at 3.05 Å resolution, revealing structural differences between the E. coli and T. thermophilus enzymes [Mermershtain11].

The reaction mechanism of PheRS includes the formation of an aminoacyl adenylate intermediate, which then serves as the animo acid donor in the aminoacyl-tRNA synthetase reaction [Lagerkvist77]. Binding of tRNAPhe to PheRS induces a conformational change in the tRNA [Favre79] as well as in PheRS [Holler81]. Aminoacylation is limited by the kinetics of a conformational change of the PheRS-Phe-tRNAPhe complex [Baltzinger82, Baltzinger82a]. PheRS can aminoacylate a synthetic substrate with a deoxyribose backbone (tDNA) [Khan88a].

Specificity determinants within tRNAPhe that are important for recognition by PheRS, for attenuation, and for editing have been identified [Ankilova75, Vlassov78, Vacher85, Delamarche87, Wilson89, Pages90, Pallanck91, Peterson92, Peterson93, Moor94, Peterson94, Ling07]. A synthetically constructed tRNAPhe(AAA) is not a good substrate for PheRS [Gavini92]. Specificity determinants and residues within PheRS that are important for catalytic activity have been investigated [Hountondji87]. The Ala294 residue of the α subunit is involved in binding phenylalanine and influences amino acid specificity by determining of the size of the binding pocket [Ibba94].

A proofreading mechanism hydrolyzes a PheRS-tyrosine adenylate complex and Tyr-tRNAPhe [Ibba94, Roy04a]. The editing site localizes to the B3/B4 domain of the β subunit [Roy04a]. PheRS of E. coli B contains a proofreading activity which deacylates misacylated Ile-tRNAPhe [Yarus72, Gabius83]. The post-transfer editing activity of PheRS is not essential for growth, but it is required for survival under oxidative stress conditions. This may be due to its ability to edit meta-tyrosine, a metabolic byproduct of the oxidation of phenylalanine [Bullwinkle14].

Expression of pheST is derepressed by an attenuation mechanism when the level of aminoacylated tRNAPhe is low [Fayat83, Springer83, Trudel84, Springer87] and by high levels of PheRS [Springer85].

A mutant with temperature-sensitive PheRS was isolated [Eidlic65].

PheRS is an antimicrobial drug target. Phenyl-thiazolylurea-sulfonamides act by inhibiting PheRS; novel inhibitors of the enzyme have been isolated [Abibi14].

Reviews: [Ibba00, Perona12]

Citations: [Bartmann75a]

Molecular Weight: 250 kD (experimental) [Ducruix83]

GO Terms:

Biological Process: GO:0006432 - phenylalanyl-tRNA aminoacylation Inferred from experiment [Comer76]
Molecular Function: GO:0004826 - phenylalanine-tRNA ligase activity Inferred from experiment [Fayat74]

Credits:
Last-Curated ? 01-Jul-2014 by Keseler I , SRI International


Enzymatic reaction of: phenylalanyl-tRNA synthetase

Synonyms: PheRS

EC Number: 6.1.1.20

tRNAphe + L-phenylalanine + ATP + H+ <=> L-phenylalanyl-tRNAphe + AMP + diphosphate

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 physiologically favored in the direction shown.

In Pathways: tRNA charging

Summary:
Equilibrium constants at various Mg2+ concentrations have been measured [Airas07].

Cofactors or Prosthetic Groups: Mg2+ [Airas96, Favre79]

Inhibitors (Competitive): 3-phenylpropanoate [Mulivor73] , phenyl-thiazolylurea-sulfonamides [Beyer04] , N-benzylbenzamidine [Danenberg75] , benzylguanidine [Danenberg75] , 2-phenylacetamidine [Danenberg75] , phenylalaninol [Mulivor73] , benzyl alcohol [Mulivor73]

Inhibitors (Unknown Mechanism): Zn2+ [Mayaux81]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
ATP
9.0
[Gabius82, BRENDA14]
ATP
130.0
[Hecht74]
tRNAphe
0.22
[Peterson92]
tRNAphe
2.2, 2.7
0.077, 0.82
[Roy06, BRENDA14]
L-phenylalanine
3.2
[Hecht74]
L-phenylalanine
5.3
3.34
[Roy06, BRENDA14]
L-phenylalanine
2.0
199.0
[Reynolds10, BRENDA14]

T(opt): 43 °C [BRENDA14, Bobkova92]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 39 -> 148
[UniProt09]
UniProt: tRNA-binding;
Sequence-Conflict 93
[Mechulam85, UniProt10]
Alternate sequence: A → T; UniProt: (in Ref. 1; CAA23565);
Sequence-Conflict 141 -> 142
[Mechulam85, UniProt10]
Alternate sequence: AP → VR; UniProt: (in Ref. 1; CAA23565);
Sequence-Conflict 186 -> 189
[Mechulam85, UniProt10]
Alternate sequence: PLVQ → AAGN; UniProt: (in Ref. 1; CAA23565);
Conserved-Region 401 -> 476
[UniProt10a]
UniProt: B5;
Metal-Binding-Site 454
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 460
[UniProt10a]
UniProt: Magnesium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 463
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 464
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 481
[Mechulam85, UniProt10]
Alternate sequence: A → R; UniProt: (in Ref. 1; CAA23565);
Sequence-Conflict 698
[Mechulam85, UniProt10]
Alternate sequence: R → G; UniProt: (in Ref. 1; CAA23565);
Conserved-Region 701 -> 794
[UniProt09]
UniProt: FDX-ACB;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1713 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10710; confirmed by SwissProt match.


References

Abibi14: Abibi A, Ferguson AD, Fleming PR, Gao N, Hajec LI, Hu J, Laganas VA, McKinney DC, McLeod SM, Prince DB, Shapiro AB, Buurman ET (2014). "The Role of a Novel Auxiliary Pocket in Bacterial Phenylalanyl-tRNA Synthetase Druggability." J Biol Chem. PMID: 24936059

Airas07: Airas RK (2007). "Magnesium dependence of the measured equilibrium constants of aminoacyl-tRNA synthetases." Biophys Chem 131(1-3);29-35. PMID: 17889423

Airas96: Airas RK (1996). "Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli." Eur J Biochem 240(1);223-31. PMID: 8797857

Ankilova75: Ankilova VN, Vlassov VV, Knorre DG, Melamed NV, Nuzdihna NA (1975). "Involvement of the D-stem of tRNAPhe (E. coli) in interaction with phenylalanyl-tRNA synthetase as shown by chemical modification." FEBS Lett 60(1);168-71. PMID: 776674

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

Baltzinger82: Baltzinger M, Holler E (1982). "Kinetics of acyl transfer ribonucleic acid complexes of Escherichia coli phenylalanyl-tRNA synthetase. A conformational change is rate limiting in catalysis." Biochemistry 21(10);2460-7. PMID: 7046786

Baltzinger82a: Baltzinger M, Holler E (1982). "Catalytic mechanism of phenylalanyl-tRNA synthetase of Escherichia coli K10. Conformational change and tRNAPhe phenylalanylation are concerted." Biochemistry 21(10);2467-76. PMID: 7046787

Bartmann75: Bartmann P, Hanke T, Holler E (1975). "Active site stoichiometry of L-phenylalanine: tRNA ligase from Escherichia coli K(-10)." J Biol Chem 250(19);7668-74. PMID: 170267

Bartmann75a: Bartmann P, Hanke T, Holler E (1975). "L-phenylalanine:tRNA ligase of Escherichia coli K10. A rapid kinetic investigation of the catalytic reaction." Biochemistry 14(22);4777-86. PMID: 1101957

Beyer04: Beyer D, Kroll HP, Endermann R, Schiffer G, Siegel S, Bauser M, Pohlmann J, Brands M, Ziegelbauer K, Haebich D, Eymann C, Brotz-Oesterhelt H (2004). "New class of bacterial phenylalanyl-tRNA synthetase inhibitors with high potency and broad-spectrum activity." Antimicrob Agents Chemother 48(2);525-32. PMID: 14742205

Bobkova91: Bobkova EV, Mashanov-Golikov AV, Wolfson A, Ankilova VN, Lavrik OI (1991). "Comparative study of subunits of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus." FEBS Lett 290(1-2);95-8. PMID: 1915899

Bobkova92: Bobkova EV, Stepanov VG, Lavrik OI (1992). "A comparative study of the relationship between thermostability and function of phenylalanyl-tRNA synthetases from Escherichia coli and Thermus thermophilus." FEBS Lett 302(1);54-6. PMID: 1587354

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

Bullwinkle14: Bullwinkle T, Reynolds NM, Raina M, Moghal AB, Matsa E, Rajkovic A, Kayadibi H, Fazlollahi F, Ryan C, Howitz N, Faull KF, Lazazzera B, Ibba M (2014). "Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code." Elife ;e02501. PMID: 24891238

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Comer76: Comer MM, Bock A (1976). "Genes for the alpha and beta subunits of the phenylalanyl-transfer ribonucleic acid synthetase of Escherichia coli." J Bacteriol 127(2);923-33. PMID: 783122

Cusack91: Cusack S, Hartlein M, Leberman R (1991). "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases." Nucleic Acids Res 19(13);3489-98. PMID: 1852601

Danenberg75: Danenberg PV, Santi DV (1975). "Inhibition of phenylalanyl-tRNA synthetase by aromatic guanidines and amidines." J Med Chem 18(5);528-30. PMID: 1097688

Delamarche87: Delamarche C, Vacher J, Buckingham RH (1987). "Mutants affecting tRNA(Phe) from Escherichia coli. Studies of the suppression of thermosensitive phenylalanyl-tRNA synthetase." Eur J Biochem 168(2);365-9. PMID: 3311746

Dessen83: Dessen P, Ducruix A, Hountondji C, May RP, Blanquet S (1983). "Neutron scattering study of the binding of tRNAPhe to Escherichia coli phenylalanyl-tRNA synthetase." Biochemistry 22(2);281-4. PMID: 6337625

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

Ducruix83: Ducruix A, Hounwanou N, Reinbolt J, Boulanger Y, Blanquet S (1983). "Purification and reversible subunit dissociation of overproduced Escherichia coli phenylalanyl-tRNA synthetase." Biochim Biophys Acta 741(2);244-50. PMID: 6360212

Eidlic65: Eidlic L, Neidhardt FC (1965). "Protein and nucleic acid synthesis in two mutants of Escherichia coli with temperature-sensitive aminoacyl ribonucleic acid synthetases." J Bacteriol 89;706-11. PMID: 14273649

Eriani90: Eriani G, Delarue M, Poch O, Gangloff J, Moras D (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs." Nature 347(6289);203-6. PMID: 2203971

Favre79: Favre A, Ballini JP, Holler E (1979). "Phenylalanyl-tRNA synthetase induced conformational change of Escherichia coli tRNA phe." Biochemistry 18(13);2887-95. PMID: 383142

Fayat74: Fayat G, Blanquet S, Dessen P, Batelier G, Waller JP (1974). "The molecular weight and subunit composition of phenylalanyl-tRNA synthetase from Escherichia coli K-12." Biochimie 56(1);35-41. PMID: 4603142

Fayat83: Fayat G, Mayaux JF, Sacerdot C, Fromant M, Springer M, Grunberg-Manago M, Blanquet S (1983). "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20." J Mol Biol 171(3);239-61. PMID: 6317865

Gabius82: Gabius HJ, Freist W, Cramer F (1982). "Phenylalanyl-tRNA synthetases from hen liver cytoplasm and mitochondria, yeast cytoplasm and mitochondria, and from Escherichia coli: substrate specificity relationship with regard to ATP analogs." Hoppe Seylers Z Physiol Chem 363(10);1241-6. PMID: 6754571

Gabius83: Gabius HJ, von der Haar F, Cramer F (1983). "Evolutionary aspects of accuracy of phenylalanyl-tRNA synthetase. A comparative study with enzymes from Escherichia coli, Saccharomyces cerevisiae, Neurospora crassa, and turkey liver using phenylalanine analogues." Biochemistry 22(10);2331-9. PMID: 6222761

Gavini92: Gavini N, Pulakat L (1992). "The tRNA species for redundant genetic codons NNU and NNC. A thought on the absence of phenylalanine tRNA with AAA anticodon in Escherichia coli." J Biol Chem 267(4);2240-3. PMID: 1370814

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."

Hecht74: Hecht SM, Hawrelak SD (1974). "Interaction of glycyl-L-phenylalanine with Escherichia coli phenylalanyl-tRNA synthetase." Biochemistry 13(24);4967-75. PMID: 4373046

Hennecke76: Hennecke H (1976). "Use of mutant enzymes to demonstrate the presence of two active sites on phenylalanyl-tRNA synthetase from Eschericia coli." FEBS Lett 72(1);182-6. PMID: 793866

Holler81: Holler E, Wang CC, Ford NC (1981). "Detection of ligand-induced conformational changes in phenylalanyl-tRNA synthetase of Escherichia coli K10 by laser light scattering." Biochemistry 20(4);861-7. PMID: 7011376

Hountondji87: Hountondji C, Schmitter JM, Beauvallet C, Blanquet S (1987). "Affinity labeling of Escherichia coli phenylalanyl-tRNA synthetase at the binding site for tRNAPhe." Biochemistry 26(17);5433-9. PMID: 2823880

Ibba00: Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis." Annu Rev Biochem 69;617-50. PMID: 10966471

Ibba94: Ibba M, Kast P, Hennecke H (1994). "Substrate specificity is determined by amino acid binding pocket size in Escherichia coli phenylalanyl-tRNA synthetase." Biochemistry 33(23);7107-12. PMID: 8003476

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Khan88a: Khan AS, Roe BA (1988). "Aminoacylation of synthetic DNAs corresponding to Escherichia coli phenylalanine and lysine tRNAs." Science 241(4861);74-9. PMID: 2455342

Khodyreva85: Khodyreva SN, Moor NA, Ankilova VN, Lavrik OI (1985). "Phenylalanyl-tRNA synthetase from E. coli MRE-600: analysis of the active site distribution on the enzyme subunits by affinity labelling." Biochim Biophys Acta 830(2);206-12. PMID: 3893548

Krauss75: Krauss G, Pingoud A, Boehme D, Riesner D, Peters F, Maas G (1975). "Equivalent and non-equivalent binding sites for +RNA on aminoacyl-tRNA synthetases." Eur J Biochem 55(3);517-29. PMID: 1100384

Lagerkvist77: Lagerkvist U, Akesson B, Branden R (1977). "Aminoacyl adenylate, a normal intermediate or a dead end in aminoacylation of transfer ribonucleic acid." J Biol Chem 252(3);1002-6. PMID: 320199

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lavrik82: Lavrik OI, Moor NA, Khodyreva SN (1982). "Phenylalanyl-tRNA synthetase from E. coli MRE-600: localization of the phenylalanine binding sites on the subunits by affinity reagents." Mol Biol Rep 8(2);123-6. PMID: 7043240

Ling07: Ling J, Roy H, Ibba M (2007). "Mechanism of tRNA-dependent editing in translational quality control." Proc Natl Acad Sci U S A 104(1);72-7. PMID: 17185419

Mayaux81: Mayaux JF, Blanquet S (1981). "Binding of zinc to Escherichia coli phenylalanyl transfer ribonucleic acid synthetase. Comparison with other aminoacyl transfer ribonucleic acid synthetases." Biochemistry 20(16);4647-54. PMID: 6794600

Mayaux84: Mayaux JF, Springer M, Graffe M, Fromant M, Fayat G (1984). "IS4 transposition in the attenuator region of the Escherichia coli pheS,T operon." Gene 30(1-3);137-46. PMID: 6096210

Mayaux85: Mayaux JF, Fayat G, Panvert M, Springer M, Grunberg-Manago M, Blanquet S (1985). "Control of phenylalanyl-tRNA synthetase genetic expression. Site-directed mutagenesis of the pheS, T operon regulatory region in vitro." J Mol Biol 184(1);31-44. PMID: 3162032

Mechulam85: Mechulam Y, Fayat G, Blanquet S (1985). "Sequence of the Escherichia coli pheST operon and identification of the himA gene." J Bacteriol 163(2);787-91. PMID: 2991205

Mermershtain11: Mermershtain I, Finarov I, Klipcan L, Kessler N, Rozenberg H, Safro MG (2011). "Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP." Protein Sci 20(1);160-7. PMID: 21082706

Moor94: Moor NA, Repkova MN, Yamkovoy VI, Lavrik OI (1994). "Alterations at the 3'-CCA end of Escherichia coli and Thermus thermophilus tRNA(Phe) do not abolish their acceptor activity." FEBS Lett 351(2);241-2. PMID: 8082771

Mulivor73: Mulivor R, Rappaport HP (1973). "Analysis of the binding of phenylalanine to phenylalanyl-tRNA synthetase." J Mol Biol 76(1);123-34. PMID: 4578095

Pages90: Pages D, Buckingham RH (1990). "Mutants of pheV in Escherichia coli affecting control by attenuation of the pheS, T and pheA operons. Two distinct mechanisms for de-attenuation." J Mol Biol 216(1);17-24. PMID: 2231729

Pallanck91: Pallanck L, Schulman LH (1991). "Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo." Proc Natl Acad Sci U S A 88(9);3872-6. PMID: 2023934

Perona12: Perona JJ, Hadd A (2012). "Structural diversity and protein engineering of the aminoacyl-tRNA synthetases." Biochemistry 51(44);8705-29. PMID: 23075299

Peterson92: Peterson ET, Uhlenbeck OC (1992). "Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase." Biochemistry 31(42);10380-9. PMID: 1420156

Peterson93: Peterson ET, Blank J, Sprinzl M, Uhlenbeck OC (1993). "Selection for active E. coli tRNA(Phe) variants from a randomized library using two proteins." EMBO J 12(7);2959-67. PMID: 7687542

Peterson94: Peterson ET, Pan T, Coleman J, Uhlenbeck OC (1994). "In vitro selection of small RNAs that bind to Escherichia coli phenylalanyl-tRNA synthetase." J Mol Biol 242(3);186-92. PMID: 8089840

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reynolds10: Reynolds NM, Ling J, Roy H, Banerjee R, Repasky SE, Hamel P, Ibba M (2010). "Cell-specific differences in the requirements for translation quality control." Proc Natl Acad Sci U S A 107(9);4063-8. PMID: 20160120

Roy04a: Roy H, Ling J, Irnov M, Ibba M (2004). "Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase." EMBO J 23(23);4639-48. PMID: 15526031

Roy06: Roy H, Ibba M (2006). "Phenylalanyl-tRNA synthetase contains a dispensable RNA-binding domain that contributes to the editing of noncognate aminoacyl-tRNA." Biochemistry 45(30);9156-62. PMID: 16866361

Russell71: Russell RR, Pittard AJ (1971). "Mutants of Escherichia coli unable to make protein at 42 C." J Bacteriol 108(2);790-8. PMID: 4942764

Springer83: Springer M, Trudel M, Graffe M, Plumbridge J, Fayat G, Mayaux JF, Sacerdot C, Blanquet S, Grunberg-Manago M (1983). "Escherichia coli phenylalanyl-tRNA synthetase operon is controlled by attenuation in vivo." J Mol Biol 171(3);263-79. PMID: 6317866

Springer85: Springer M, Mayaux JF, Fayat G, Plumbridge JA, Graffe M, Blanquet S, Grunberg-Manago M (1985). "Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon." J Mol Biol 181(4);467-78. PMID: 3158742

Springer87: Springer M, Graffe M, Mayaux JF, Dardel F, Fayat G, Blanquet S, Grunberg-Manago M (1987). "Open reading frames in the control regions of the phenylalanyl-tRNA synthetase operon of E. coli." Biochimie 69(10);1065-70. PMID: 3126825

Trudel84: Trudel M, Springer M, Graffe M, Fayat G, Blanquet S, Grunberg-Manago M (1984). "Regulation of E.coli phenylalanyl-tRNA synthetase operon in vivo." Biochim Biophys Acta 782(1);10-7. PMID: 6426518

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UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Vacher85: Vacher J, Springer M, Buckingham RH (1985). "Functional mutants of phenylalanine transfer RNA from Escherichia coli." EMBO J 4(2);509-13. PMID: 3894009

Vlassov78: Vlassov VV, Khodyreva SN (1978). "Equilibrium screening-dialysis investigation of the nucleotide sequences in the tRNAPhe recognized by phenylalanyl-tRNA synthetase (Escherichia coli)." FEBS Lett 96(1);95-8. PMID: 365576

Wertheimer88: Wertheimer SJ, Klotsky RA, Schwartz I (1988). "Transcriptional patterns for the thrS-infC-rplT operon of Escherichia coli." Gene 63(2);309-20. PMID: 2838394

Wilson89: Wilson RK, Roe BA (1989). "Presence of the hypermodified nucleotide N6-(delta 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA." Proc Natl Acad Sci U S A 86(2);409-13. PMID: 2643111

Yarus72: Yarus M (1972). "Phenylalanyl-tRNA synthetase and isoleucyl-tRNA Phe : a possible verification mechanism for aminoacyl-tRNA." Proc Natl Acad Sci U S A 69(7);1915-9. PMID: 4558664

Other References Related to Gene Regulation

Lemke11: Lemke JJ, Sanchez-Vazquez P, Burgos HL, Hedberg G, Ross W, Gourse RL (2011). "Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA." Proc Natl Acad Sci U S A 108(14);5712-7. PMID: 21402902

Lesage90: Lesage P, Truong HN, Graffe M, Dondon J, Springer M (1990). "Translated translational operator in Escherichia coli. Auto-regulation in the infC-rpmI-rplT operon." J Mol Biol 213(3);465-75. PMID: 2191140

Mayaux83: Mayaux JF, Fayat G, Fromant M, Springer M, Grunberg-Manago M, Blanquet S (1983). "Structural and transcriptional evidence for related thrS and infC expression." Proc Natl Acad Sci U S A 80(20);6152-6. PMID: 6353409

Partridge09: Partridge JD, Bodenmiller DM, Humphrys MS, Spiro S (2009). "NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility." Mol Microbiol 73(4);680-94. PMID: 19656291

Springer86: Springer M, Graffe M, Butler JS, Grunberg-Manago M (1986). "Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli." Proc Natl Acad Sci U S A 83(12);4384-8. PMID: 3086882


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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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