Hfq

• 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

Categories containing this gene/protein

RNA chaperones

The gene

Basic information

• Locus tag: BSU17340

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:

Database entries

• Structure: 3HSB (complex with an RNA aptamer) PubMed

• UniProt: O31796

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: hfq PubMed

• Expression browser: hfq PubMed

• Sigma factor:

• Regulation:
  • repressed by glucose (7.7-fold) PubMed
  • expression (mRNA levels) is quite constant during growth in minimal medium PubMed
  • the Hfq protein amount increases upon transition to stationary phase PubMed

• 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:

References

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)