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
Sequences	Protein DNA DNA_with_flanks
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

• BsubCyc: BSU17340

• 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

• BsubCyc: BSU17340

• 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:
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 46 PubMed

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)