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Escherichia coli K-12 substr. MG1655 Polypeptide: phenylalanyl-tRNA synthetase α-chain

Gene: pheS Accession Numbers: EG10709 (EcoCyc), b1714, ECK1712

Synonyms: phe-act

Regulation Summary Diagram

Regulation summary diagram for pheS

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

The α subunit of PheRS contains the phenylalanine binding site [Hennecke75, Lavrik82] within the conserved motif 2 and motif 3 of the protein [Kast91, Kast91a]. It interacts with the 3'-adenosine of tRNAPhe [Hountondji87].

Isolated α subunits exist primarily as dimers [Bobkova91].

The pheS5 mutant allele causes temperature-sensitive PheRS activity [Eidlic65, Kast92]. Intragenic supressors of the pheS5 mutation have been isolated and analyzed [Ponmani14].

Citations: [Comer76]

Gene Citations: [Fayat83, Wertheimer88, Springer85a, Mechulam85, Mayaux84, Springer83, Mayaux85, Trudel84]

Locations: cytosol

Map Position: [1,795,983 <- 1,796,966] (38.71 centisomes, 139°)
Length: 984 bp / 327 aa

Molecular Weight of Polypeptide: 36.832 kD (from nucleotide sequence), 38 kD (experimental) [Ducruix83]

Unification Links: ASAP:ABE-0005722, CGSC:400, DIP:DIP-6878N, EchoBASE:EB0703, EcoGene:EG10709, EcoliWiki:b1714, Mint:MINT-1229741, ModBase:P08312, OU-Microarray:b1714, PortEco:pheS, Pride:P08312, Protein Model Portal:P08312, RefSeq:NP_416229, RegulonDB:EG10709, SMR:P08312, String:511145.b1714, Swiss-Model:P08312, UniProt:P08312

Relationship Links: InterPro:IN-FAMILY:IPR002319, InterPro:IN-FAMILY:IPR004188, InterPro:IN-FAMILY:IPR004529, InterPro:IN-FAMILY:IPR006195, InterPro:IN-FAMILY:IPR010978, InterPro:IN-FAMILY:IPR022911, Pfam:IN-FAMILY:PF01409, Pfam:IN-FAMILY:PF02912, Prosite:IN-FAMILY:PS50862

Gene-Reaction Schematic

Gene-Reaction Schematic

Genetic Regulation Schematic

Genetic regulation schematic for pheS

GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0006432 - phenylalanyl-tRNA aminoacylation [GOA06, GOA01a, Gaudet10, Eidlic65]
Inferred by computational analysisGO:0006412 - translation [UniProtGOA11a]
Inferred by computational analysisGO:0006418 - tRNA aminoacylation for protein translation [GOA01a]
Inferred by computational analysisGO:0043039 - tRNA aminoacylation [GOA01a]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Rajagopala14, Lasserre06, Butland05]
Inferred by computational analysisGO:0000049 - tRNA binding [GOA01a]
Inferred by computational analysisGO:0000166 - nucleotide binding [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0000287 - magnesium ion binding [GOA06]
Inferred by computational analysisGO:0004812 - aminoacyl-tRNA ligase activity [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0004826 - phenylalanine-tRNA ligase activity [GOA06, GOA01, GOA01a, Gaudet10]
Inferred by computational analysisGO:0005524 - ATP binding [UniProtGOA11a, GOA06, GOA01a]
Inferred by computational analysisGO:0016874 - ligase activity [UniProtGOA11a]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11a]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, Lasserre06]
Inferred from experimentInferred by computational analysisGO:0005829 - cytosol [DiazMejia09, Ishihama08, LopezCampistrou05]
Inferred from experimentGO:0009328 - phenylalanine-tRNA ligase complex [Fayat74]

MultiFun Terms: information transferprotein relatedamino acid -activation

Essentiality data for pheS knockouts:

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

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)

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) [Khan88b].

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 [Springer85a].

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:
Inferred from experimentGO:0006432 - phenylalanyl-tRNA aminoacylation [Comer76]
Molecular Function:
Inferred from experimentGO:0004826 - phenylalanine-tRNA ligase activity [Fayat74]

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

Enzymatic reaction of: phenylalanyl-tRNA synthetase

Inferred from experiment

Synonyms: PheRS

EC Number:

a tRNAphe + L-phenylalanine + ATP + H+ → an L-phenylalanyl-[tRNAphe] + AMP + diphosphate

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: tRNA charging

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]
a tRNAphe 0.22 [Peterson92]
a tRNAphe 2.2, 2.7 0.077, 0.82 [Roy06, BRENDA14]
L-phenylalanine 3.2 [Hecht74]
L-phenylalanine 5.3 3.34 0.63 [Roy06, BRENDA14]
L-phenylalanine 2.0 199.0 99.5 [Reynolds10, BRENDA14]

T(opt): 43 °C [BRENDA14, Bobkova92]

Sequence Features

Protein sequence of phenylalanyl-tRNA synthetase alpha-chain with features indicated

Feature Class Location Citations Comment
Pfam PF02912 17 -> 87
Inferred by computational analysis[Finn14]
Phe_tRNA-synt_N : Aminoacyl tRNA synthetase class II, N-terminal domain
Sequence-Conflict 74
Inferred by curator[Blattner97, UniProt15]
UniProt: (in Ref. 2; CAA23564 and 4; AAA51469).
Pfam PF01409 92 -> 326
Inferred by computational analysis[Finn14]
tRNA-synt_2d : tRNA synthetases class II core domain (F)
Extrinsic-Sequence-Variant 98
Inferred from experiment[Kast92]
UniProt: In thermosensitive mutant pheS5; might cause subunit disaggregation due to electrostatic repulsion..
Extrinsic-Sequence-Variant 191
Inferred from experiment[Kast91a]
UniProt: Decreased affinity for Phe..
Metal-Binding-Site 252
Inferred by computational analysis[UniProt15]
UniProt: Magnesium.

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Units

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b1714 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10709; confirmed by SwissProt match.


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 289(31);21651-62. 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

Blattner97: Blattner FR, Plunkett G, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y (1997). "The complete genome sequence of Escherichia coli K-12." Science 277(5331);1453-74. PMID: 9278503

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.

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

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

Hennecke75: Hennecke H, Bock A (1975). "Altered alpha subunits in phenylalanyl-tRNA synthetases from p-fluorophenylalanine-resistant strains of Escherichis coli." Eur J Biochem 55(2);431-7. PMID: 1104359

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

Kast91: Kast P, Hennecke H (1991). "Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations." J Mol Biol 222(1);99-124. PMID: 1942071

Kast91a: Kast P, Wehrli C, Hennecke H (1991). "Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases." FEBS Lett 293(1-2);160-3. PMID: 1959653

Kast92: Kast P, Keller B, Hennecke H (1992). "Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37." J Bacteriol 174(5);1686-9. PMID: 1537809

Khan88b: Khan AS, Roe BA (1988). "Aminoacylation of synthetic DNAs corresponding to Escherichia coli phenylalanine and lysine tRNAs." Science 241(4861);74-9. PMID: 2455342

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

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

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

Ponmani14: Ponmani T, Munavar MH (2014). "G673 could be a novel mutational hot spot for intragenic suppressors of pheS5 lesion in Escherichia coli." Microbiologyopen 3(3);369-82. PMID: 24811065

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

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

Springer85a: 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

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords 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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