Difference between revisions of "LicT"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''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:''' | + | * '''Protein family:''' BglG family of antiterminators |
− | * '''Paralogous protein(s):''' | + | * '''Paralogous protein(s):''' [[SacY]], [[GlcT]], [[SacT]] |
=== Extended information on the protein === | === Extended information on the protein === |
Revision as of 12:45, 8 February 2009
- Description: write here
Gene name | licT |
Synonyms | |
Essential | |
Product | transcriptional antiterminator (BglG family) |
Function | required for substrate-dependent induction and catabolite repression of bglPH |
MW, pI | 32 kDa, 5.944 |
Gene length, protein length | 831 bp, 277 aa |
Immediate neighbours | |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
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)
- Protein family: BglG family of antiterminators
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Josef Deutscher, Paris-Grignon, France
Michael Hecker, Greifswald, Germany Homepage
Your additional remarks
References
- Schnetz, K., Stülke, J., Gertz, S., Krüger, S., Krieg, M., Hecker, M. & Rak, B. (1996) LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family. J. Bacteriol. 178: 1971-1979. PubMed
- Lindner, C., Galinier, A., Hecker, M. & Deutscher, J. (1999) Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31, 995-1006 . PubMed
- Lindner, C., Hecker, M., Le Coq, D. & Deutscher, J. (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184, 4819-4828 . PubMed
- Krüger, S., Gertz, S. & Hecker, M. Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression. J. Bacteriol. 178, 2637-2644 (1996). PubMed
- Declerck N, Dutartre H, Receveur V, Dubois V, Royer C, Aymerich S, van Tilbeurgh H (2001) Dimer stabilzation upon activation of the transcriptional antiterminator LicT. J Mol Biol 314:671-681. PubMed
- Graille, M. et al. Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J. Biol. Chem. 280, 14780-14789 (2005). PubMed
- Tortosa, P., Declerck, N., Dutartre, H., Lindner, C., Deutscher, J., and Le Coq, D. (2001) Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY. Mol Microbiol 41: 1381-1393. PubMed
- van Tilbeurgh H, Le Coq D, Declerck N (2001) Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator. EMBO J 20:3789-3799. PubMed
- Yang Y, Declerck N, Manival X, Aymerich S, Kochoyan M (2002) Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT. EMBO J 21:1987-1997. PubMed
- Aymerich, S. and Steinmetz, M. (1992) Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family. Proc. Natl. Acad. Sci. USA 89, 10410-10414. PubMed
- Declerck, N., Vincent, F., Hoh, F., Aymerich, S. and van Tilbeurgh, H. (1999) RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domains from SacY and LicT. J. Mol. Biol. 294, 389-402. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed