Escherichia coli K-12 substr. MG1655 tRNA: tRNApheV

Gene: pheV Accession Numbers: EG30065 (EcoCyc), b2967, ECK2962

Synonyms: pheC

Superclasses: a tRNAphe

Regulation Summary Diagram: ?

Regulation summary diagram for pheV

tRNA(pheV) is one of two phenylalanine tRNAs.

tRNAs are the adapters that allow synthesis of proteins from mRNAs. Each tRNA carries a specific amino acid to the ribosome for protein synthesis. There, the tRNA recognizes an RNA codon with its own three-nucleotide anticodon, thus allowing synthesis of a specific peptide based on an mRNA template.

tRNAs are processed to their active, mature forms by RNA cleavage and by modification of their bases. RNA cleavage consists of removal of both 5' and 3' extensions in a multistep process involving many RNases [Morl01]. RNases taking part in tRNA processing include ribonuclease E, RNase BN, RNase D, ribonuclease II, and RNase T. tRNAs are also subject to a wide variety of base modifications catalyzed by proteins such as tRNA-dihydrouridine synthase A, tRNA(i6A37) synthase, isopentenyl-adenosine A37 tRNA methylthiolase, tRNA-specific 2-thiouridylase, fused 5-methylaminomethyl-2-thiouridine-forming methyltransferase and FAD-dependent demodification enzyme, tRNA-guanine transglycosylase, tRNA m7G46 methyltransferase, tRNA pseudouridine 13 synthase, tRNA pseudouridine 65 synthase, tRNA pseudouridine 55 synthase, tRNA pseudouridine synthase I, tRNA (Gm18) 2'-O-methyltransferase, and tRNA m5U54 methyltransferase.

A solution structure of tRNA(phe) pseudouridylated at position U32 (ψ32) has been analyzed, indicating that ψ32 preserves the integrity of the anticodon stem [CabelloVillegas05]. The structure of tRNA(phe) has also been evaluated via methyl C-13 NMR and ESR, revealing that it switches between two conformations depending on pH, magnesium concentration and other factors [Agris80, Bondarev82, Hyde85].

Mature tRNAs are linked via a 3' CCA sequence to their cognate amino acid in an ATP-dependent fashion by the appropriate amino-acid-tRNA synthetase, as shown in the tRNA charging. Subsequently, these charged tRNAs interact with the ribosome and template mRNA to generate polypeptides. The discovery of the role of tRNA in protein synthesis is reviewed in detail in [Siekevitz81].

Following UVA irradiation, tRNA(phe) is acylated at one-tenth the normal rate, causing a growth defect [Blondel88].

Map Position: [3,108,388 -> 3,108,463] (67.0 centisomes, 241°)
Length: 76 bp

Anticodon: GAA

Reactions known to consume the compound:

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

Reactions known to produce the compound:

tRNA processing :
a tRNA precursor with a short 3' extension → an uncharged tRNA + n a nucleoside 5'-monophosphate
a tRNA precursor with a short 3' extension + n phosphate → an uncharged tRNA + n a ribonucleoside diphosphate
a tRNA precursor with a 5' extension + H2O → an uncharged tRNA + a single-stranded RNA

Not in pathways:
an N-modified aminoacyl-[tRNA] + H2O → an uncharged tRNA + an N-modified amino acid + 2 H+
a D-aminoacyl-[tRNA] + H2O → a D-amino acid + an uncharged tRNA + 2 H+

Not in pathways:
a tRNA precursor + H2O → a tRNA + a nucleoside 5'-monophosphate

tRNA processing :
a tRNA precursor with a 5' extension and a short 3' extension + H2O → a tRNA precursor with a short 3' extension + a single-stranded RNA
a tRNA precursor with a 5' extension + H2O → an uncharged tRNA + a single-stranded RNA

Not in pathways:
YhaV endonuclease degradation substrate mRNA + H2O → 2 a single-stranded RNA
an mRNA + H2O → a single-stranded RNA + a single-stranded RNA
an mRNA + H2O → a single-stranded RNA + a single-stranded RNA
RNase E degradation substrate mRNA + n H2O → n a single-stranded RNA
YhaV endonuclease degradation substrate rRNA + H2O → 2 a single-stranded RNA
RNase III mRNA processing substrate + 2 H2O → RNase III processing product mRNA + 2 a single-stranded RNA
23S rRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]
an mRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]
RNase G degradation substrate mRNA + H2O → 2 a single-stranded RNA
9S rRNA + 2 H2O → 5S rRNA + 2 a single-stranded RNA
RNase E mRNA processing substrate + n H2O → RNase E processing product mRNA + n a single-stranded RNA

Reactions known to both consume and produce the compound:

Not in pathways:
a single-stranded RNA + phosphate ↔ a single-stranded RNA + a nucleoside diphosphate

In Reactions of unknown directionality:

Not in pathways:
rRNA[periplasmic space] = 2 a single-stranded RNA[periplasmic space]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for pheV

Unification Links: ASAP:ABE-0009738 , CGSC:18058 , EchoBASE:EB4228 , EcoGene:EG30065 , EcoliWiki:b2967 , OU-Microarray:b2967 , PortEco:pheV , RegulonDB:EG30065

GO Terms:

Molecular Function: GO:0030533 - triplet codon-amino acid adaptor activity
Cellular Component: GO:0005737 - cytoplasm
GO:0005829 - cytosol

MultiFun Terms: information transfer RNA related tRNA

Transcription Units regulated by related protein L-phenylalanyl-tRNApheV (2 total):

Transcription-unit diagram

Transcription-unit diagram

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b2967 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG30065.

Last-Curated ? 26-Apr-2006 by Shearer A , SRI International


Agris80: Agris PF, Schmidt PG (1980). "Structure of transfer RNA by carbon NMR: resolution of single carbon resonances from 13C-enriched, purified species." Nucleic Acids Res 8(9);2085-91. PMID: 6159600

Blondel88: Blondel MO, Favre A (1988). "tRNAPhe and tRNAPro are the near-ultraviolet molecular targets triggering the growth delay effect." Biochem Biophys Res Commun 150(3);979-86. PMID: 2449211

Bondarev82: Bondarev GN, Isaev-Ivanov VV, Isaeva-Ivanova LS, Kirillov SV, Kleiner AR, Lepekhin AF, Odinzov VB, Fomichev VN (1982). "Study on conformational states of Escherichia coli tRNAPhe in solution by a modulation-free ESR-spectrometer." Nucleic Acids Res 10(3);1113-26. PMID: 6278435

CabelloVillegas05: Cabello-Villegas J, Nikonowicz EP (2005). "Solution structure of psi32-modified anticodon stem-loop of Escherichia coli tRNAPhe." Nucleic Acids Res 33(22);6961-71. PMID: 16377777

Hyde85: Hyde EI, Reid BR (1985). "NMR studies of ion binding to Escherichia coli tRNAPhe." Biochemistry 24(16);4315-25. PMID: 3902084

Morl01: Morl M, Marchfelder A (2001). "The final cut. The importance of tRNA 3'-processing." EMBO Rep 2(1);17-20. PMID: 11252717

Siekevitz81: Siekevitz P, Zamecnik PC (1981). "Ribosomes and protein synthesis." J Cell Biol 91(3 Pt 2);53s-65s. PMID: 7033244

Other References Related to Gene Regulation

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Ow02: Ow MC, Kushner SR (2002). "Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli." Genes Dev 16(9);1102-15. PMID: 12000793

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Jul 28, 2015, biocyc12.