Difference between revisions of "LicT"

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(Extended information on the protein)
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
 
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** K(D) for the RAT-RNA: 10 nM {{PubMed|10610766}}
 
* '''Domains:'''  
 
* '''Domains:'''  
 
** N-terminal RNA binding domain [http://www.ncbi.nlm.nih.gov/pubmed/10610766?dopt=Abstract Pubmed]
 
** N-terminal RNA binding domain [http://www.ncbi.nlm.nih.gov/pubmed/10610766?dopt=Abstract Pubmed]

Revision as of 19:40, 31 January 2013

Gene name licT
Synonyms
Essential no
Product transcriptional antiterminator (BglG family)
Function control of beta-glucan and beta-glucoside utilization
Gene expression levels in SubtiExpress: licT
Interactions involving this protein in SubtInteract: LicT
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 32 kDa, 5.944
Gene length, protein length 831 bp, 277 aa
Immediate neighbours bglS, yxiP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LicT context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LicT expression.png















Categories containing this gene/protein

utilization of specific carbon sources, transcription factors and their control, RNA binding regulators, phosphoproteins

This gene is a member of the following regulons

The LicT regulon: bglP-bglH-yxiE, bglS

The gene

Basic information

  • Locus tag: BSU39080

Phenotypes of a mutant

no expression of the bglP-bglH operon

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: binding to the mRNAs of bglS and the bglP-bglH operon, causes transcription antitermination (in presence of salicin and absence of glucose)

Extended information on the protein

  • Kinetic information:
    • K(D) for the RAT-RNA: 10 nM PubMed
  • Domains:
    • N-terminal RNA binding domain Pubmed
    • 2xPRD (PTS regulation domains) PubMed
  • Modification:
    • phosphorylation at His-100 in PRD-1 by phosphorylated BglP, inhibits LicT antitermination activity
    • phosphorylation at His-207 and/or His-269 in PRD-2 by His-P-HPr, stimulates LicT antitermination activity
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1L1C (complex with RAT), 1TLV (PRDs)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP427 (licTS, erm), available in the Stülke lab
  • Expression vector:
    • for expression, purification of both PRDs in E. coli with N-terminal His-tag, in pWH844: pGP165, available in Stülke lab
    • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag, in pWH844: pGP315, available in Stülke lab
    • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP572, available in Stülke lab
  • lacZ fusion:
  • GFP fusion: GP1225 (spc, based on pGP1870), available in the Stülke lab
  • YFP fusion: GP1229 (spc, based on pGP1871), available in the Stülke lab
  • FLAG-tag construct: GP1221 (spc, based on pGP1331), available in the Stülke lab
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

Josef Deutscher, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

Michael Hecker, Greifswald, Germany Homepage

Your additional remarks

References

Additional publications: PubMed

Original description


Control of LicT activity


Structural analysis of LicT

Hélène Déméné, Thierry Ducat, Karine De Guillen, Catherine Birck, Stéphane Aymerich, Michel Kochoyan, Nathalie Declerck
Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.
J Biol Chem: 2008, 283(45);30838-49
[PubMed:18682383] [WorldCat.org] [DOI] (P p)

Marc Graille, Cong-Zhao Zhou, Véronique Receveur-Bréchot, Bruno Collinet, Nathalie Declerck, Herman van Tilbeurgh
Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.
J Biol Chem: 2005, 280(15);14780-9
[PubMed:15699035] [WorldCat.org] [DOI] (P p)

N Declerck, H Dutartre, V Receveur, V Dubois, C Royer, S Aymerich, H van Tilbeurgh
Dimer stabilization upon activation of the transcriptional antiterminator LicT.
J Mol Biol: 2001, 314(4);671-81
[PubMed:11733988] [WorldCat.org] [DOI] (P p)

H van Tilbeurgh, D Le Coq, N Declerck
Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.
EMBO J: 2001, 20(14);3789-99
[PubMed:11447120] [WorldCat.org] [DOI] (P p)


LicT-RNA interaction