LicT

• Description: transcriptional antiterminator of the bglP-bglH operon and the bglS gene
  
  

Gene name	licT
Synonyms
Essential	no
Product	transcriptional antiterminator (BglG family)
Function	substrate-dependent induction of bglP-bglH and bglS
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 This image was kindly provided by SubtiList

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]

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)

• Protein family: transcriptional antiterminator BglG family of antiterminators (according to Swiss-Prot)

• Paralogous protein(s): SacY, GlcT, SacT

Extended information on the protein

• Kinetic information:

• 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:

• Interactions: PtsH-LicT

• Localization:

Database entries

• Structure: 1L1C (complex with RAT), 1TLV (PRDs)

• UniProt: P39805

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: licT-bglS PubMed

• Sigma factor: SigA PubMed

• 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:

• 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

References

Original description

Control of LicT activity

Cordula Lindner, Michael Hecker, Dominique Le Coq, Josef Deutscher
Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon.
J Bacteriol: 2002, 184(17);4819-28
[PubMed:12169607] [WorldCat.org] [DOI] (P p)

P Tortosa, N Declerck, H Dutartre, C Lindner, J Deutscher, D Le Coq
Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY.
Mol Microbiol: 2001, 41(6);1381-93
[PubMed:11580842] [WorldCat.org] [DOI] (P p)

C Lindner, A Galinier, M Hecker, J Deutscher
Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation.
Mol Microbiol: 1999, 31(3);995-1006
[PubMed:10048041] [WorldCat.org] [DOI] (P p)

S Krüger, S Gertz, M Hecker
Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression.
J Bacteriol: 1996, 178(9);2637-44
[PubMed:8626332] [WorldCat.org] [DOI] (P p)

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

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)

Yinshan Yang, Nathalie Declerck, Xavier Manival, Stéphane Aymerich, Michel Kochoyan
Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT.
EMBO J: 2002, 21(8);1987-97
[PubMed:11953318] [WorldCat.org] [DOI] (P p)

N Declerck, F Vincent, F Hoh, S Aymerich, H van Tilbeurgh
RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.
J Mol Biol: 1999, 294(2);389-402
[PubMed:10610766] [WorldCat.org] [DOI] (P p)

S Aymerich, M Steinmetz
Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family.
Proc Natl Acad Sci U S A: 1992, 89(21);10410-4
[PubMed:1279678] [WorldCat.org] [DOI] (P p)