Difference between revisions of "Hfq"
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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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| + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ymaH_1867373_1867594_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:hfq_expression.png|500px]] | ||
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Revision as of 10:10, 19 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
| |
Expression at a glance PubMed
| |
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)
