Difference between revisions of "Hfq"
(→Original publications) |
|||
(33 intermediate revisions by 5 users not shown) | |||
Line 13: | Line 13: | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown | |style="background:#ABCDEF;" align="center"|'''Function''' || unknown | ||
+ | |- | ||
+ | |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] | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 8 kDa, 8.698 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 8 kDa, 8.698 | ||
Line 20: | Line 22: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[miaA]]'', ''[[ymzC]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[miaA]]'', ''[[ymzC]]'' | ||
|- | |- | ||
− | | | + | |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 DNA_with_flanks] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:ymaH_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:ymaH_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |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]] | ||
|- | |- | ||
|} | |} | ||
__TOC__ | __TOC__ | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/> | ||
− | + | = [[Categories]] containing this gene/protein = | |
+ | {{SubtiWiki category|[[RNA chaperones]]}} | ||
+ | |||
+ | = This gene is a member of the following [[regulons]] = | ||
=The gene= | =The gene= | ||
Line 40: | Line 51: | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU17340&redirect=T BSU17340] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
Line 46: | Line 58: | ||
=== Additional information=== | === Additional information=== | ||
+ | |||
+ | |||
Line 70: | Line 84: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU17340&redirect=T BSU17340] | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3HSB 3HSB] (complex with an RNA aptamer) {{PubMed|22053080}} |
− | * ''' | + | * '''UniProt:''' [http://www.uniprot.org/uniprot/O31796 O31796] |
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU17340] | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU17340] | ||
Line 88: | Line 103: | ||
=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''[[hfq]]'' {{PubMed|23457461}} |
+ | |||
+ | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ymaH_1867373_1867594_1 hfq] {{PubMed|22383849}} | ||
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
− | * '''Regulation:''' repressed by glucose (7.7-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | + | * '''Regulation:''' |
+ | ** repressed by glucose (7.7-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
+ | ** expression (mRNA levels) is quite constant during growth in minimal medium {{PubMed|23457461}} | ||
+ | ** the Hfq protein amount increases upon transition to stationary phase {{PubMed|23457461}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
+ | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 46 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = | ||
− | * '''Mutant:''' | + | * '''Mutant:''' GP22 (cat), available in the [[Jörg Stülke]]'s lab |
* '''Expression vector:''' | * '''Expression vector:''' | ||
− | * '''lacZ fusion:''' | + | * '''lacZ fusion:''' pGP460 (in [[pAC7]]), available in [[Jörg Stülke]]'s lab |
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
− | * '''two-hybrid system:''' | + | * '''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:''' | * '''Antibody:''' | ||
Line 117: | Line 141: | ||
=References= | =References= | ||
+ | ==Reviews== | ||
+ | <pubmed> 17395525 15009882 21760622 </pubmed> | ||
− | <pubmed>12850135, </pubmed> | + | ==Original publications== |
+ | <pubmed>12850135, 20445260 23457461 22965117,22053080 24932523 25150227 25915524</pubmed> | ||
+ | [[Category:Protein-coding genes]] |
Latest revision as of 15:41, 29 April 2015
- 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
- BsubCyc: BSU17340
- 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
- BsubCyc: BSU17340
- UniProt: O31796
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications
Tatiana Rochat, Olivier Delumeau, Nara Figueroa-Bossi, Philippe Noirot, Lionello Bossi, Etienne Dervyn, Philippe Bouloc
Tracking the Elusive Function of Bacillus subtilis Hfq.
PLoS One: 2015, 10(4);e0124977
[PubMed:25915524]
[WorldCat.org]
[DOI]
(I e)
Alexander R Kovach, Kirsten E Hoff, John T Canty, Jillian Orans, Richard G Brennan
Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes.
RNA: 2014, 20(10);1548-59
[PubMed:25150227]
[WorldCat.org]
[DOI]
(I p)
Hermann Hämmerle, Fabian Amman, Branislav Večerek, Jörg Stülke, Ivo Hofacker, Udo Bläsi
Impact of Hfq on the Bacillus subtilis transcriptome.
PLoS One: 2014, 9(6);e98661
[PubMed:24932523]
[WorldCat.org]
[DOI]
(I e)
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)