hfq:Quickview: Difference between revisions

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{|   id="G49aee8b7dd8ab"  class=" tableEdit New_Quickview_Table" 
 
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!{{table_heading_style}} |Gene Name
!align=left {{table_heading_style}} |Standard Name
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[[hfq:Gene|''hfq]]'' (synonyms: ''ECK4168, b4172, JW4130, HF-I, HF-1'')<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>
''hfq''
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!{{table_heading_style}} |Product(s)  
!align=left {{table_heading_style}} |Gene Synonym(s)
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[[hfq:Gene_Product(s)|Hfq product]]<ref name='LIB:Riley_2006'/>: HF-I, host factor for RNA phage Q beta replication product, B4172 product, HF-I product, host factor I product
''ECK4168, b4172, JW4130, HF-I, HF-1''<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>
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!{{table_heading_style}} |Description
!align=left {{table_heading_style}} |Product Desc.
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RNA-binding protein that affects many cellular processes; homolog of mammalian Sm/Sm-like proteins<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>  
RNA-binding protein that affects many cellular processes; homolog of mammalian Sm/Sm-like proteins<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;


Component of [[:Category:Complex:HF-I, host factor for RNA phage Q &beta; replication|HF-I, host factor for RNA phage Q &beta; replication]]<ref name='LIB:EcoCyc11.1'/>
Component of [[:Category:Complex:HF-I, host factor for RNA phage Q beta replication|HF-I, host factor for RNA phage Q β replication]]<ref name='LIB:EcoCyc11.1'/>


Global regulator of sRNA function; host factor for RNA phage Q beta replication; HF-I; DNA- and RNA-binding protein; RNA chaperone; multiple regulatory roles: destabilzes ompA mRNA, improves rpoS translation, sRNA DsrA co-factor; binds RNAP; ATPase<ref name='LIB:EcoGene'/>
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!align=left {{table_heading_style}} |Product Synonyms(s)
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''HF-I, host factor for RNA phage Q beta replication<ref name='LIB:Riley_2006'/>, B4172<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Hfq<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, HF-I<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, host factor I<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> , ECK4168, JW4130, b4172''
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!align=left {{table_heading_style}} |Function from GO
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<GO_nr />
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!{{table_heading_style}} |Knock-Out Phenotype
!align=left {{table_heading_style}} |Knock-Out Phenotype
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!{{table_heading_style}} |Regulation/Expression
!align=left {{table_heading_style}} |Regulation/Expression
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transcription unit(s): [[:Category:Txn_unit:yjeFE-amiB-mutL-miaA-hfq-hflXKC|yjeFE-amiB-mutL-miaA-hfq-hflXKC]]<ref name='LIB:EcoCyc10.6'/>, ORF55-ORF17-amiB-mutL-miaA-hfq-hflXKC  
transcription unit(s): [[:Category:Txn_unit:yjeFE-amiB-mutL-miaA-hfq-hflXKC|yjeFE-amiB-mutL-miaA-hfq-hflXKC]]<ref name='LIB:EcoCyc10.6'/>, ORF55-ORF17-amiB-mutL-miaA-hfq-hflXKC  
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!{{table_heading_style}} |Regulation/Activity
!align=left {{table_heading_style}} |Regulation/Activity
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!align=left {{table_heading_style}} |Quick Links
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[[File:porteco.png|link=http://porteco.org/AjaxSearch.jsp?searchString=hfq&s=search]] [[File:EcoCyc.gif|link=http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=EG10438]] [[File:regulondb.jpg|link=http://regulondb.ccg.unam.mx/gene?term=ECK120000431&organism=ECK12&format=jsp&type=gene ]] <br/><br/> [[File:dnadisplay.png|link=http://ecoliwiki.net/tools/display_dna.php?gene=hfq&loc=MG1655%3A4398311..4398619,W3110%3A4404968..4405276,DH10B%3A4498673..4498981,REL606%3A4378443..4378751,BW2952%3A4337046..4337354]] [[File:proteindisplay.png|link=http://ecoliwiki.net/tools/display_protein.php?f=NC_000913&start=4337046&end=4337354&gene=hfq&aa=makgqslqdpflnalrrervpvsiylvngiklqgqiesfdqfvillkntvsqmvykhaistvvpsrpvshhsnnagggtssnyhhgssaqntsaqqdseete]]&nbsp;&nbsp;  [[File:pubmed.jpg|link=http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=hfq+AND+escherichia+coli]]&nbsp;&nbsp;  [[File:textpresso.jpg|link=http://textpresso.tamu.edu/cgi-bin/textpresso/search?q=hfq]]&nbsp;&nbsp;
 
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The C-terminal of Hfq is not necessary for hexamerization.  RNA binding is located primarily at the N-terminal. Hfq has intrinsic ATPase activity (Sukhodolets, 2003; Arluison, 2007).<ref name='LIB:EcoGene'/>
Hfq enhances RNA-RNA pairing. <ref name='PMID:11804582'/>


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==References==
==References==
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Latest revision as of 21:49, 27 May 2013

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
References Suggestions
Standard Name

hfq

Gene Synonym(s)

ECK4168, b4172, JW4130, HF-I, HF-1[1][2]

Product Desc.

RNA-binding protein that affects many cellular processes; homolog of mammalian Sm/Sm-like proteins[2][3];

Component of HF-I, host factor for RNA phage Q β replication[3]

Global regulator of sRNA function; host factor for RNA phage Q beta replication; HF-I; DNA- and RNA-binding protein; RNA chaperone; multiple regulatory roles: destabilzes ompA mRNA, improves rpoS translation, sRNA DsrA co-factor; binds RNAP; ATPase[4]

Product Synonyms(s)

HF-I, host factor for RNA phage Q beta replication[1], B4172[2][1], Hfq[2][1], HF-I[2][1], host factor I[2][1] , ECK4168, JW4130, b4172

Function from GO

<GO_nr />

Knock-Out Phenotype
Regulation/Expression

transcription unit(s): yjeFE-amiB-mutL-miaA-hfq-hflXKC[2], ORF55-ORF17-amiB-mutL-miaA-hfq-hflXKC

Regulation/Activity
Quick Links



        

See Help:Quickview for help with entering information in the Quickview table.

Notes

[back to top]


The C-terminal of Hfq is not necessary for hexamerization. RNA binding is located primarily at the N-terminal. Hfq has intrinsic ATPase activity (Sukhodolets, 2003; Arluison, 2007).[4]

Hfq enhances RNA-RNA pairing. [5]


References

[back to top]


  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.0 4.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Zhang, A et al. (2002) The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs. Mol. Cell 9 11-22 PubMed