Escherichia coli K-12 substr. MG1655 tRNA: tRNAthrW

Gene: thrW Accession Numbers: EG30104 (EcoCyc), b0244, ECK0245

Synonyms: tRNAThr2(CGU)

Superclasses: a tRNAthr

Regulation Summary Diagram: ?

Regulation summary diagram for thrW

tRNA(thrW) is one of four threonine 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 solution structure of tRNA(thr) both alone and in contact with synthetase has been chemically and enzymatically evaluated [Theobald88].

The relative abundances of the different tRNA(thr) species have been examined [Comer82].

Certain temperature-sensitive htrB mutants are complemented by thrW [Mohri03].

Map Position: [262,095 -> 262,170] (5.65 centisomes, 20°)
Length: 76 bp

Anticodon: CGU

Reactions known to consume the compound:

tRNA charging :
a tRNAthr + L-threonine + ATP + H+ → an L-threonyl-[tRNAthr] + 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 thrW

Unification Links: ASAP:ABE-0000834 , CGSC:10363 , EchoBASE:EB4267 , EcoGene:EG30104 , EcoliWiki:b0244 , OU-Microarray:b0244 , PortEco:thrW , RegulonDB:EG30104

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-threonyl-tRNAthrW (1 total):

Transcription-unit diagram

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b0244 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG30104.

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


Comer82: Comer MM (1982). "Threonine tRNAs and their genes in Escherichia coli." Mol Gen Genet 187(1);132-7. PMID: 6761541

Mohri03: Mohri Y, Goto S, Nakahigashi K, Inokuchi H (2003). "tRNA2Thr complements temperature sensitivity caused by null mutations in the htrB gene in Escherichia coli." J Bacteriol 185(5);1726-9. PMID: 12591892

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

Theobald88: Theobald A, Springer M, Grunberg-Manago M, Ebel JP, Giege R (1988). "Tertiary structure of Escherichia coli tRNA(3Thr) in solution and interaction of this tRNA with the cognate threonyl-tRNA synthetase." Eur J Biochem 175(3);511-24. PMID: 2457500

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.

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 Wed May 6, 2015, biocyc11.