Difference between revisions of "Hfq"
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= This gene is a member of the following [[regulons]] =  | = This gene is a member of the following [[regulons]] =  | ||
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=The gene=  | =The gene=  | ||
Revision as of 17:33, 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
Michael Dambach, Irnov Irnov, Wade C Winkler  
Association of RNAs with Bacillus subtilis Hfq. 
PLoS One: 2013, 8(2);e55156 
[PubMed:23457461]
  [WorldCat.org]
 [DOI]
 (I p)
Nicola Horstmann, Jillian Orans, Poul Valentin-Hansen, Samuel A Shelburne, Richard G Brennan  
Structural mechanism of Staphylococcus aureus Hfq binding to an RNA A-tract. 
Nucleic Acids Res: 2012, 40(21);11023-35 
[PubMed:22965117]
  [WorldCat.org]
 [DOI]
 (I p)
Tatsuhiko Someya, Seiki Baba, Mai Fujimoto, Gota Kawai, Takashi Kumasaka, Kouji Nakamura  
Crystal structure of Hfq from Bacillus subtilis in complex with SELEX-derived RNA aptamer: insight into RNA-binding properties of bacterial Hfq. 
Nucleic Acids Res: 2012, 40(4);1856-67 
[PubMed:22053080]
  [WorldCat.org]
 [DOI]
 (I p)
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)

