Difference between revisions of "Hfq"
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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]] | + | |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|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU17340]] |
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Revision as of 13:26, 16 May 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 |
| Sequences | Protein DNA DNA_with_flanks |
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
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)
