Difference between revisions of "Hfq"
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* '''Operon:''' | * '''Operon:''' | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ymaH_1867373_1867594_1 hfq] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' | ||
* '''Regulation:''' repressed by glucose (7.7-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | * '''Regulation:''' repressed by glucose (7.7-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = |
Revision as of 09:33, 13 April 2012
- Description: RNA chaperone
Gene name | hfq |
Synonyms | ymaH |
Essential | no |
Product | RNA chaperone |
Function | unknown |
MW, pI | 8 kDa, 8.698 |
Gene length, protein length | 219 bp, 73 aa |
Immediate neighbours | miaA, ymzC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU17340
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: hfq 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
- UniProt: O31796
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation: repressed by glucose (7.7-fold) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP22 (cat), available in the Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Jörg Vogel, Ben F Luisi
Hfq and its constellation of RNA.
Nat Rev Microbiol: 2011, 9(8);578-89
[PubMed:21760622]
[WorldCat.org]
[DOI]
(I e)
Richard G Brennan, Todd M Link
Hfq structure, function and ligand binding.
Curr Opin Microbiol: 2007, 10(2);125-33
[PubMed:17395525]
[WorldCat.org]
[DOI]
(P p)
Poul Valentin-Hansen, Maiken Eriksen, Christina Udesen
The bacterial Sm-like protein Hfq: a key player in RNA transactions.
Mol Microbiol: 2004, 51(6);1525-33
[PubMed:15009882]
[WorldCat.org]
[DOI]
(P p)
Original publications
Additional publications: PubMed
Seiki Baba, Tatsuhiko Someya, Gota Kawai, Kouji Nakamura, Takashi Kumasaka
Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 5);563-6
[PubMed:20445260]
[WorldCat.org]
[DOI]
(I p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)