LiaR

From SubtiWiki
Revision as of 17:35, 13 September 2013 by Jstuelk (talk | contribs) (References)
Jump to: navigation, search
Gene name liaR
Synonyms yvqC
Essential no
Product two-component response regulator
Function regulation of the liaI-liaH-liaG-liaF-liaS-liaR

operon in response to bacitracin

Gene expression levels in SubtiExpress: liaR

operon in response to bacitracin

Interactions involving this protein in SubtInteract: LiaR
MW, pI 22 kDa, 4.956
Gene length, protein length 633 bp, 211 aa
Immediate neighbours gerAC, liaS
Sequences Protein DNA DNA_with_flanks
Genetic context
YvqC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LiaR expression.png















Categories containing this gene/protein

transcription factors and their control, resistance against oxidative and electrophile stress, resistance against toxins/ antibiotics, phosphoproteins

This gene is a member of the following regulons

LiaR regulon

The LiaR regulon

The gene

Basic information

  • Locus tag: BSU33080

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: regulation of the liaI-liaH-liaG-liaF-liaS-liaR operon in response to bacitracin
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on a Asp residue by LiaS
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage


Your additional remarks

References

Sara Kesel, Andreas Mader, Carolin Höfler, Thorsten Mascher, Madeleine Leisner
Immediate and heterogeneous response of the LiaFSR two-component system of Bacillus subtilis to the peptide antibiotic bacitracin.
PLoS One: 2013, 8(1);e53457
[PubMed:23326432] [WorldCat.org] [DOI] (I p)

Karen Schrecke, Sina Jordan, Thorsten Mascher
Stoichiometry and perturbation studies of the LiaFSR system of Bacillus subtilis.
Mol Microbiol: 2013, 87(4);769-88
[PubMed:23279150] [WorldCat.org] [DOI] (I p)

Diana Wolf, Patricia Domínguez-Cuevas, Richard A Daniel, Thorsten Mascher
Cell envelope stress response in cell wall-deficient L-forms of Bacillus subtilis.
Antimicrob Agents Chemother: 2012, 56(11);5907-15
[PubMed:22964256] [WorldCat.org] [DOI] (I p)

Tina Wecke, Tobias Bauer, Henning Harth, Ulrike Mäder, Thorsten Mascher
The rhamnolipid stress response of Bacillus subtilis.
FEMS Microbiol Lett: 2011, 323(2);113-23
[PubMed:22092710] [WorldCat.org] [DOI] (I p)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Diana Wolf, Falk Kalamorz, Tina Wecke, Anna Juszczak, Ulrike Mäder, Georg Homuth, Sina Jordan, Janine Kirstein, Michael Hoppert, Birgit Voigt, Michael Hecker, Thorsten Mascher
In-depth profiling of the LiaR response of Bacillus subtilis.
J Bacteriol: 2010, 192(18);4680-93
[PubMed:20639339] [WorldCat.org] [DOI] (I p)

Andriansjah Rukmana, Takuya Morimoto, Hiroki Takahashi, Giyanto, Naotake Ogasawara
Assessment of transcriptional responses of Bacillus subtilis cells to the antibiotic enduracidin, which interferes with cell wall synthesis, using a high-density tiling chip.
Genes Genet Syst: 2009, 84(4);253-67
[PubMed:20057163] [WorldCat.org] [DOI] (P p)

Tina Wecke, Daniela Zühlke, Ulrike Mäder, Sina Jordan, Birgit Voigt, Stefan Pelzer, Harald Labischinski, Georg Homuth, Michael Hecker, Thorsten Mascher
Daptomycin versus Friulimicin B: in-depth profiling of Bacillus subtilis cell envelope stress responses.
Antimicrob Agents Chemother: 2009, 53(4);1619-23
[PubMed:19164157] [WorldCat.org] [DOI] (I p)

Anna-Barbara Hachmann, Esther R Angert, John D Helmann
Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin.
Antimicrob Agents Chemother: 2009, 53(4);1598-609
[PubMed:19164152] [WorldCat.org] [DOI] (I p)

Eva Rietkötter, Diana Hoyer, Thorsten Mascher
Bacitracin sensing in Bacillus subtilis.
Mol Microbiol: 2008, 68(3);768-85
[PubMed:18394148] [WorldCat.org] [DOI] (I p)

Bronwyn G Butcher, Yi-Pin Lin, John D Helmann
The yydFGHIJ operon of Bacillus subtilis encodes a peptide that induces the LiaRS two-component system.
J Bacteriol: 2007, 189(23);8616-25
[PubMed:17921301] [WorldCat.org] [DOI] (I p)

Sina Jordan, Eva Rietkötter, Mark A Strauch, Falk Kalamorz, Bronwyn G Butcher, John D Helmann, Thorsten Mascher
LiaRS-dependent gene expression is embedded in transition state regulation in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 8);2530-2540
[PubMed:17660417] [WorldCat.org] [DOI] (P p)

Hanne-Leena Hyyryläinen, Milla Pietiäinen, Tuula Lundén, Anna Ekman, Marika Gardemeister, Sanna Murtomäki-Repo, Haike Antelmann, Michael Hecker, Leena Valmu, Matti Sarvas, Vesa P Kontinen
The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 7);2126-2136
[PubMed:17600057] [WorldCat.org] [DOI] (P p)

Sina Jordan, Anja Junker, John D Helmann, Thorsten Mascher
Regulation of LiaRS-dependent gene expression in bacillus subtilis: identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system.
J Bacteriol: 2006, 188(14);5153-66
[PubMed:16816187] [WorldCat.org] [DOI] (P p)

Thorsten Mascher, Sara L Zimmer, Terry-Ann Smith, John D Helmann
Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis.
Antimicrob Agents Chemother: 2004, 48(8);2888-96
[PubMed:15273097] [WorldCat.org] [DOI] (P p)

Mélanie A Hamon, Nicola R Stanley, Robert A Britton, Alan D Grossman, Beth A Lazazzera
Identification of AbrB-regulated genes involved in biofilm formation by Bacillus subtilis.
Mol Microbiol: 2004, 52(3);847-60
[PubMed:15101989] [WorldCat.org] [DOI] (P p)

Thorsten Mascher, Neil G Margulis, Tao Wang, Rick W Ye, John D Helmann
Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon.
Mol Microbiol: 2003, 50(5);1591-604
[PubMed:14651641] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)