Difference between revisions of "Hfq"

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|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
 
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
 
|-
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU17340 hfq]
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU17340 hfq]
 
|-
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 8 kDa, 8.698   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 8 kDa, 8.698   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[miaA]]'', ''[[ymzC]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[miaA]]'', ''[[ymzC]]''
 
|-
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13618&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU17340 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU17340 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU17340 Advanced_DNA]
 
|-
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ymaH_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ymaH_context.gif]]

Revision as of 12:54, 13 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 Advanced_DNA
Genetic context
YmaH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Hfq expression.png















Categories containing this gene/protein

RNA chaperones

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

  • Structure: 3HSB (complex with an RNA aptamer) PubMed
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • 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

  • Expression vector:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), 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)