Escherichia coli K-12 substr. MG1655 tRNA: tRNAtyrT

Gene: tyrT Accession Numbers: EG30106 (EcoCyc), b1231, ECK1226

Synonyms: tyrTalpha, supFsupO, Su-3, Su-4, su(c), suIII, supC

Superclasses: a tRNAtyr

Regulation Summary Diagram: ?

Regulation summary diagram for tyrT

tRNA(tyrT) is one of three tyrosine 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.

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].

The 5' leader of tRNA(tyrT) is processed by RNase E [Soderbom05].

Map Position: [1,286,761 <- 1,286,845] (27.73 centisomes, 100°)
Length: 85 bp

Anticodon: GUA

Reactions known to consume the compound:

tRNA charging :
a tRNAtyr + L-tyrosine + ATP + H+ → an L-tyrosyl-[tRNAtyr] + 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:
D-tyrosyl-tRNATyr + H2O = a tRNAtyr + D-tyrosine

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 tyrT

Unification Links: ASAP:ABE-0004136 , CGSC:53 , EchoBASE:EB4269 , EcoGene:EG30106 , EcoliWiki:b1231 , OU-Microarray:b1231 , PortEco:tyrT , RegulonDB:EG30106

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

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b1231 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG30106.

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


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

Soderbom05: Soderbom F, Svard SG, Kirsebom LA (2005). "RNase E cleavage in the 5' leader of a tRNA precursor." J Mol Biol 352(1);22-7. PMID: 16081101

Other References Related to Gene Regulation

Auner03: Auner H, Buckle M, Deufel A, Kutateladze T, Lazarus L, Mavathur R, Muskhelishvili G, Pemberton I, Schneider R, Travers A (2003). "Mechanism of transcriptional activation by FIS: role of core promoter structure and DNA topology." J Mol Biol 331(2);331-44. PMID: 12888342

Lazarus93: Lazarus LR, Travers AA (1993). "The Escherichia coli FIS protein is not required for the activation of tyrT transcription on entry into exponential growth." EMBO J 12(6);2483-94. PMID: 7685276

Li97c: Li S, Waters R (1997). "Induction and repair of cyclobutane pyrimidine dimers in the Escherichia coli tRNA gene tyrT: Fis protein affects dimer induction in the control region and suppresses preferential repair in the coding region of the transcribed strand, except in a short region near the transcription start site." J Mol Biol 271(1);31-46. PMID: 9300053

Maciag11: Maciag A, Peano C, Pietrelli A, Egli T, De Bellis G, Landini P (2011). "In vitro transcription profiling of the {sigma}S subunit of bacterial RNA polymerase: re-definition of the {sigma}S regulon and identification of {sigma}S-specific promoter sequence elements." Nucleic Acids Res 39(13);5338-55. PMID: 21398637

Muskhelishvili95: Muskhelishvili G, Travers AA, Heumann H, Kahmann R (1995). "FIS and RNA polymerase holoenzyme form a specific nucleoprotein complex at a stable RNA promoter." EMBO J 14(7);1446-52. PMID: 7537215

Muskhelishvili97: Muskhelishvili G, Buckle M, Heumann H, Kahmann R, Travers AA (1997). "FIS activates sequential steps during transcription initiation at a stable RNA promoter." EMBO J 16(12);3655-65. PMID: 9218806

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

Pemberton02: Pemberton IK, Muskhelishvili G, Travers AA, Buckle M (2002). "FIS modulates the kinetics of successive interactions of RNA polymerase with the core and upstream regions of the tyrT promoter." J Mol Biol 318(3);651-63. PMID: 12054813

Travers01: Travers A, Schneider R, Muskhelishvili G (2001). "DNA supercoiling and transcription in Escherichia coli: The FIS connection." Biochimie 83(2);213-7. PMID: 11278071

Report Errors or Provide Feedback
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 Aug 4, 2015, BIOCYC14B.