U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

leuS leucine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947497, updated on 2-May-2024

Summary

Go to the top of the page Help
Gene symbol
leuS
Gene description
leucine--tRNA ligase
Primary source
ASAP:ABE-0002196
Locus tag
b0642
See related
ECOCYC:EG10532
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0635; syl
Summary
Leucyl-tRNA synthetase (LeuRS) 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. [More information is available at EcoCyc: EG10532].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (672201..674783, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene nicotinate-nucleotide adenylyltransferase Neighboring gene DNA polymerase III subunit delta Neighboring gene lipopolysaccharide assembly protein LptE Neighboring gene DUF1451 domain-containing protein YbeL Neighboring gene Sel1 repeat-containing protein YbeQ

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Zinc is the molecular "switch" that controls the catalytic cycle of bacterial leucyl-tRNA synthetase. Kumar M, et al. J Inorg Biochem, 2015 Jan. PMID 25450019
  2. The physiological target for LeuRS translational quality control is norvaline. Cvetesic N, et al. EMBO J, 2014 Aug 1. PMID 24935946, Free PMC Article
  3. The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation. Tan M, et al. Nucleic Acids Res, 2013 May 1. PMID 23585282, Free PMC Article
  4. tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase. Tan M, et al. J Biol Chem, 2010 Jan 29. PMID 19940155, Free PMC Article
  5. A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase. Mascarenhas AP, et al. FEBS Lett, 2009 Nov 3. PMID 19796639, Free PMC Article

See all (62) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Mechanism of discrimination of isoleucyl-tRNA synthetase against nonproteinogenic alpha-aminobutyrate and its fluorinated analogues.
    Title: Mechanism of discrimination of isoleucyl-tRNA synthetase against nonproteinogenic α-aminobutyrate and its fluorinated analogues.
  2. Zinc is the molecular "switch" that controls the catalytic cycle of bacterial leucyl-tRNA synthetase
    Title: Zinc is the molecular "switch" that controls the catalytic cycle of bacterial leucyl-tRNA synthetase.
  3. In vitro assays showed that acetyl-phosphate nonenzymatically acetylates EcLeuRS and EcArgRS and suggested that the sirtuin class deacetylase CobB might regulate acetylation of these two enzymes. These findings imply a potential regulatory role for Lys acetylation in controlling the activity of aminoacyl-tRNA synthetases and thus protein synthesis.
    Title: Acetylation of lysine ϵ-amino groups regulates aminoacyl-tRNA synthetase activity in Escherichia coli.
  4. The prime biological function of LeuRS editing is to prevent mis-incorporation of the non-standard amino acid norvaline.
    Title: The physiological target for LeuRS translational quality control is norvaline.
  5. This work provides an assessment of how intra-molecular translocation of the tRNA CCA-tail balances the aminoacylation and editing activities of LeuRS.
    Title: The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.
  6. analysis of tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase
    Title: tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase.
  7. the functions of the CP2 domain are dependent on its location in the primary sequence of LeuRS
    Title: The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and post-transfer editing.
  8. A point mutation in CP1 of class I leucyl-tRNA synthetase inactivates deacylase activity and produces misacylated tRNA, although deletion of the entire CP1 domain also disabled the deacylase activity
    Title: CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase.
  9. identified specific residues within the beta-strand tethers that selectively impact enzyme activity, supporting the idea that beta-strand orientation is crucial for Leucyl-tRNA synthetase canonical core and CP1 domain functions
    Title: Functional segregation of a predicted "hinge" site within the beta-strand linkers of Escherichia coli leucyl-tRNA synthetase.
  10. Multiple nonstandard as well as standard amino acids were toxic to the cell when LeuRS editing was inactivated
    Title: Amino acid toxicities of Escherichia coli that are prevented by leucyl-tRNA synthetase amino acid editing.
Submit: New GeneRIF Correction See all GeneRIFs (13)

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA editing activity IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables leucine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables leucine-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables leucine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in aminoacyl-tRNA metabolism involved in translational fidelity IEA
Inferred from Electronic Annotation
more info
  
involved_in leucyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within leucyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in leucyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
  
involved_in tRNA aminoacylation for protein translation IEA
Inferred from Electronic Annotation
more info
  
involved_in translation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
leucine--tRNA ligase
NP_415175.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    672201..674783 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415175.1 leucine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415175.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A831GQJ8
    Conserved Domains (1) summary
    PRK00390
    Location:1 → 860
    leuS; leucyl-tRNA synthetase; Validated
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Other Literature Sources
Molecular Biology Databases
Research Materials