Difference between revisions of "Hfq"
| Line 102: | Line 102: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[hfq]]'' {{PubMed|23457461}} |
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ymaH_1867373_1867594_1 hfq] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ymaH_1867373_1867594_1 hfq] {{PubMed|22383849}} | ||
| Line 108: | Line 108: | ||
* '''[[Sigma factor]]:''' | * '''[[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] | ||
| + | ** expression (mRNA levels) is quite constant during growth in minimal medium {{PubMed|23457461}} | ||
| + | ** the Hfq protein amount increases upon transition to stationary phase {{PubMed|23457461}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| Line 116: | Line 119: | ||
=Biological materials = | =Biological materials = | ||
| − | * '''Mutant:''' GP22 (cat), available in the [[Stülke]] lab | + | * '''Mutant:''' GP22 (cat), available in the [[Jörg Stülke]]'s lab |
* '''Expression vector:''' | * '''Expression vector:''' | ||
| − | * '''lacZ fusion:''' pGP460 (in [[pAC7]]), available in [[Stülke]] lab | + | * '''lacZ fusion:''' pGP460 (in [[pAC7]]), available in [[Jörg Stülke]]'s lab |
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
| − | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab | + | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Jörg Stülke]]'s lab |
* '''FLAG-tag construct:''' | * '''FLAG-tag construct:''' | ||
| Line 140: | Line 143: | ||
==Original publications== | ==Original publications== | ||
| − | + | <pubmed>12850135, 20445260 23457461 22965117,22053080</pubmed> | |
| − | <pubmed>12850135, 20445260 23457461 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:53, 28 March 2013
- Description: RNA chaperone
| Gene name | hfq |
| Synonyms | ymaH |
| Essential | no |
| Product | RNA chaperone |
| Function | unknown |
| Gene expression levels in SubtiExpress: hfq | |
| 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
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP22 (cat), available in the Jörg Stülke's lab
- Expression vector:
- lacZ fusion: pGP460 (in pAC7), available in Jörg Stülke's lab
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- FLAG-tag construct:
- GP1067 (spc, based on pGP1331), available in Jörg Stülke's 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
