Difference between revisions of "TilS"

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(Original publications)
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* '''Description:''' [[trigger enzyme]], tRNAIle-lysidine synthetase and part of a transcription activator<br/><br/>
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* '''Description:''' [[trigger enzyme]], tRNAIle-lysidine synthetase (modifies C34 at the wobble position of tRNA2Ile to lysidine) and part of a transcription activator<br/><br/>
  
 
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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
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** modifies C34 at the wobble position of tRNA2Ile to lysidine
  
 
* '''Protein family:''' tRNA(Ile)-lysidine synthase family (according to Swiss-Prot)
 
* '''Protein family:''' tRNA(Ile)-lysidine synthase family (according to Swiss-Prot)

Revision as of 17:06, 17 November 2013

  • Description: trigger enzyme, tRNAIle-lysidine synthetase (modifies C34 at the wobble position of tRNA2Ile to lysidine) and part of a transcription activator

Gene name tilS
Synonyms yacA
Essential yes PubMed
Product tRNAIle-lysidine synthetase
Function tRNA modification, control of ftsH expression
Gene expression levels in SubtiExpress: tilS
Interactions involving this protein in SubtInteract: TilS
Metabolic function and regulation of this protein in SubtiPathways:
Nucleotides (regulation)
MW, pI 53 kDa, 8.317
Gene length, protein length 1416 bp, 472 aa
Immediate neighbours yabT, hprT
Sequences Protein DNA DNA_with_flanks
Genetic context
YacA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TilS expression.png















Categories containing this gene/protein

translation, transcription factors and their control, cell envelope stress proteins (controlled by SigM, V, W, X, Y), essential genes

This gene is a member of the following regulons

SigM regulon

The TilS-HprT regulon

The gene

Basic information

  • Locus tag: BSU00670

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • modifies C34 at the wobble position of tRNA2Ile to lysidine
  • Protein family: tRNA(Ile)-lysidine synthase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3A2K (from Geobacillus kaustophilus, complex with tRNA) PubMed
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Tsutomu Suzuki, Kenjyo Miyauchi
Discovery and characterization of tRNAIle lysidine synthetase (TilS).
FEBS Lett: 2010, 584(2);272-7
[PubMed:19944692] [WorldCat.org] [DOI] (I p)

Henri Grosjean, Glenn R Björk
Enzymatic conversion of cytidine to lysidine in anticodon of bacterial isoleucyl-tRNA--an alternative way of RNA editing.
Trends Biochem Sci: 2004, 29(4);165-8
[PubMed:15124629] [WorldCat.org] [DOI] (P p)

Original publications

Caroline Köhrer, Debabrata Mandal, Kirk W Gaston, Henri Grosjean, Patrick A Limbach, Uttam L Rajbhandary
Life without tRNAIle-lysidine synthetase: translation of the isoleucine codon AUA in Bacillus subtilis lacking the canonical tRNA2Ile.
Nucleic Acids Res: 2014, 42(3);1904-15
[PubMed:24194599] [WorldCat.org] [DOI] (I p)

Ta-Hui Lin, Yi-Nei Hu, Gwo-Chyuan Shaw
Two enzymes, TilS and HprT, can form a complex to function as a transcriptional activator for the cell division protease gene ftsH in Bacillus subtilis.
J Biochem: 2014, 155(1);5-16
[PubMed:24001521] [WorldCat.org] [DOI] (I p)

Céline Fabret, Etienne Dervyn, Bérengère Dalmais, Alain Guillot, Christian Marck, Henri Grosjean, Philippe Noirot
Life without the essential bacterial tRNA Ile2-lysidine synthetase TilS: a case of tRNA gene recruitment in Bacillus subtilis.
Mol Microbiol: 2011, 80(4);1062-74
[PubMed:21435031] [WorldCat.org] [DOI] (I p)

Kotaro Nakanishi, Luc Bonnefond, Satoshi Kimura, Tsutomu Suzuki, Ryuichiro Ishitani, Osamu Nureki
Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase.
Nature: 2009, 461(7267);1144-8
[PubMed:19847269] [WorldCat.org] [DOI] (I p)

Scott P Salowe, Judyann Wiltsie, Julio C Hawkins, Lisa M Sonatore
The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase.
J Biol Chem: 2009, 284(15);9656-62
[PubMed:19233850] [WorldCat.org] [DOI] (P p)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

Alison Hunt, Joy P Rawlins, Helena B Thomaides, Jeff Errington
Functional analysis of 11 putative essential genes in Bacillus subtilis.
Microbiology (Reading): 2006, 152(Pt 10);2895-2907
[PubMed:17005971] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Akiko Soma, Yoshiho Ikeuchi, Satoru Kanemasa, Kazuo Kobayashi, Naotake Ogasawara, Tomotake Ote, Jun-ichi Kato, Kimitsuna Watanabe, Yasuhiko Sekine, Tsutomu Suzuki
An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA.
Mol Cell: 2003, 12(3);689-98
[PubMed:14527414] [WorldCat.org] [DOI] (P p)