Difference between revisions of "Sandbox"

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Basura
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* '''Description:''' enolase, glycolytic/ gluconeogenic enzyme, [[universally conserved protein]]<br/><br/>
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{| align="right" border="1" cellpadding="2"
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|-
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|style="background:#ABCDEF;" align="center"|'''Gene name'''
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|''eno''
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|-
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|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
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|-
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no
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|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || enolase
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|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis/ gluconeogenesis
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|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Eno Eno]
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|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
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|-
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46,4 kDa, 4.49
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|-
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1290 bp, 430 amino acids
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|-
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvbK]]'', ''[[pgm]]''
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|-
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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:CAB15395&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|-
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|colspan="2" | '''Genetic context''' <br/> [[Image:eno_context.gif]]
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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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|}
 +
 
 +
<br/><br/><br/><br/>
 +
 
 +
__TOC__
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 +
 
 +
 
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<br/><br/><br/><br/>
 +
 
 +
 
 +
= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[carbon core metabolism]]}},
 +
{{SubtiWiki category|[[membrane proteins]]}},
 +
{{SubtiWiki category|[[phosphoproteins]]}},
 +
{{SubtiWiki category|[[universally conserved proteins]]}}
 +
 
 +
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[CggR regulon]]}}
 +
 
 +
=The gene=
 +
 
 +
=== Basic information ===
 +
* '''Locus tag:''' BSU33900
 +
 
 +
===Phenotypes of a mutant ===
 +
* no growth on LB, requires glucose and malate
 +
* essential according to Kobayashi et al. on LB  [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 +
 
 +
=== Database entries ===
 +
 
 +
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cggR-gapA-pgk-tpiA-pgm-eno.html]
 +
 
 +
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10899]
 +
 
 +
=== Additional information===
 +
 
 +
=The protein=
 +
 
 +
=== Basic information/ Evolution ===
 +
 
 +
* '''Catalyzed reaction/ biological activity:''' 2-phospho-D-glycerate = phosphoenolpyruvate + H<sub>2</sub>O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
 +
 
 +
* '''Protein family:''' enolase family (according to Swiss-Prot)
 +
 
 +
* '''Paralogous protein(s):'''
 +
 
 +
=== Extended information on the protein ===
 +
 
 +
* '''Kinetic information:''' reversible Michaelis-Menten [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed]
 +
 
 +
* '''Domains:'''
 +
** substrate binding domain (366–369)
 +
 
 +
* '''Modification:''' phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
 +
 
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* '''Cofactor(s):''' Mg2+
 +
 
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* '''Effectors of protein activity:'''
 +
** Inhibited by EDTA [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed]
 +
 
 +
* '''[[SubtInteract|Interactions]]:'''
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** forms octamers {{PubMed|22198292}}
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** part of the [[RNA degradosome]]  {{PubMed|19193632}}
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** [[Eno]]-[[PfkA]] {{PubMed|19193632}}, K(D) of the interaction: 40 nM {{PubMed|22198292}}
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** [[Eno]]-[[Rny]] {{PubMed|19193632,21803996}}, K(D) of the interaction: 100 nM {{PubMed|22198292}}
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** [[Eno]]-[[CshA]] {{PubMed|20572937}}
 +
 
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* '''[[Localization]]:'''
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** cytoplasm [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
 +
** membrane associated [http://www.ncbi.nlm.nih.gov/sites/entrez/18763711 PubMed]
 +
** exported, this requires a long, unbent α-helix (from A108 to L126)  {{PubMed|15003462,21856851}}
 +
 
 +
=== Database entries ===
 +
 
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* '''Structure:'''
 +
** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=4A3R 4A3R] {{PubMed|22198292}}
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** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1W6T 1W6T] (from ''Streptococcus pneumoniae'') {{PubMed|15476816}}
 +
 
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* '''UniProt:''' [http://www.uniprot.org/uniprot/P37869 P37869]
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU33900]
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* '''E.C. number:''' [http://www.expasy.org/enzyme/4.2.1.11 4.2.1.11]
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=== Additional information===
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* Enolase is a [[moonlighting proteins|moonlighting protein]]. [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed]
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* There are indications that this enzyme is an octamer [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed]
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* [[universally conserved protein]]
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* extensive information on the structure and enzymatic properties of Eno can be found at [http://www.proteopedia.org/wiki/index.php/Enolase Proteopedia]
 +
 
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=Expression and regulation=
 +
 
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* '''Operon:'''
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** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}}
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** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}}
 +
 
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* '''Sigma factor:''' [[SigA]] {{PubMed|11489127}}
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* '''Regulation:'''
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** expression activated by glucose (3.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] 
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** ''[[cggR]]'': induced by glycolytic substrates [[CggR]] {{PubMed|11489127}}
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** ''[[pgk]]'': constitutive {{PubMed|11489127}}
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* '''Regulatory mechanism:''' transcription repression by [[CggR]] {{PubMed|11489127}}
 +
 
 +
* '''Additional information:'''
 +
 
 +
=Biological materials =
 +
 
 +
* '''Mutant:'''
 +
** GP594 (''eno''::''cat''), available in [[Stülke]] lab
 +
** GP599 (''eno''::''erm''), available in [[Stülke]] lab
 +
** GP698 (''eno''-''[[pgm]]''::''cat''), available in [[Stülke]] lab
 +
 
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* '''Expression vector:'''
 +
** pGP1426 (expression of ''[[eno]]'' in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab
 +
** pGP1500 (expression of ''[[pgm]]'' and ''[[eno]]'' in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab
 +
** pGP563 (N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab
 +
** pGP1276 (N-terminal Strep-tag, purification from ''E. coli'', in [[pGP172]]), available in [[Stülke]] lab
 +
** pGP93 (N-terminal Strep-tag, purification from ''B. subtilis'', for [[SPINE]], in [[pGP380]]), available in [[Stülke]] lab
 +
** GP1215 (''eno''-''Strep'' ''(spc)''), purification from ''B. subtilis'', for [[SPINE]], available in [[Stülke]] lab
 +
 
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* '''lacZ fusion:'''
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** see ''[[pgk]]''
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* '''GFP fusion:''' pHT315-yfp-eno, available in [[Mijakovic]] lab
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* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
 +
 
 +
* '''FLAG-tag construct:''' GP1214 (spc, based on [[pGP1331]]), available in the [[Stülke]] lab
 +
 
 +
* '''Antibody:''' available in [[Stülke]] lab
 +
 
 +
=Labs working on this gene/protein=
 +
 
 +
[[Stülke|Jörg Stülke]], University of Göttingen, Germany
 +
[http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 +
 
 +
=Your additional remarks=
 +
 
 +
=References=
 +
==Reviews==
 +
<pubmed> 8994873 </pubmed>
 +
==Subcellular localization of enolase==
 +
'''Additional publications:''' {{PubMed|21856851}}
 +
<pubmed> 16479537 18763711 15003462 20497499 </pubmed>
 +
 
 +
==Other original publications==
 +
<pubmed> 17726680, 17218307, 12850135, 19193632, 11489127, 8021172, 17505547, 25885, 20572937 15476816 9988532 ,21803996 22198292 </pubmed>
 +
 
 +
[[Category:Protein-coding genes]]

Revision as of 15:46, 22 March 2012

Gene name eno
Synonyms
Essential no
Product enolase
Function enzyme in glycolysis/ gluconeogenesis
Interactions involving this protein in SubtInteract: Eno
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 46,4 kDa, 4.49
Gene length, protein length 1290 bp, 430 amino acids
Immediate neighbours yvbK, pgm
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Eno context.gif
This image was kindly provided by SubtiList











Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins, universally conserved proteins

This gene is a member of the following regulons

CggR regulon

The gene

Basic information

  • Locus tag: BSU33900

Phenotypes of a mutant

  • no growth on LB, requires glucose and malate
  • essential according to Kobayashi et al. on LB PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
  • Protein family: enolase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: reversible Michaelis-Menten PubMed
  • Domains:
    • substrate binding domain (366–369)
  • Modification: phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 PubMed, PubMed, PubMed
  • Cofactor(s): Mg2+
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism: transcription repression by CggR PubMed
  • Additional information:

Biological materials

  • Mutant:
    • GP594 (eno::cat), available in Stülke lab
    • GP599 (eno::erm), available in Stülke lab
    • GP698 (eno-pgm::cat), available in Stülke lab
  • Expression vector:
    • pGP1426 (expression of eno in B. subtilis, in pBQ200), available in Stülke lab
    • pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Stülke lab
    • pGP563 (N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP1276 (N-terminal Strep-tag, purification from E. coli, in pGP172), available in Stülke lab
    • pGP93 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
    • GP1215 (eno-Strep (spc)), purification from B. subtilis, for SPINE, available in Stülke lab
  • lacZ fusion:
  • GFP fusion: pHT315-yfp-eno, available in Mijakovic lab
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • FLAG-tag construct: GP1214 (spc, based on pGP1331), available in the Stülke lab
  • Antibody: available in Stülke lab

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

G H Reed, R R Poyner, T M Larsen, J E Wedekind, I Rayment
Structural and mechanistic studies of enolase.
Curr Opin Struct Biol: 1996, 6(6);736-43
[PubMed:8994873] [WorldCat.org] [DOI] (P p)

Subcellular localization of enolase

Additional publications: PubMed

Carsten Jers, Malene Mejer Pedersen, Dafni Katerina Paspaliari, Wolfgang Schütz, Christina Johnsson, Boumediene Soufi, Boris Macek, Peter Ruhdal Jensen, Ivan Mijakovic
Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates.
Mol Microbiol: 2010, 77(2);287-99
[PubMed:20497499] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Grégory Boël, Vianney Pichereau, Ivan Mijakovic, Alain Mazé, Sandrine Poncet, Sylvie Gillet, Jean-Christophe Giard, Axel Hartke, Yanick Auffray, Josef Deutscher
Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?
J Mol Biol: 2004, 337(2);485-96
[PubMed:15003462] [WorldCat.org] [DOI] (P p)


Other original publications

Joseph A Newman, Lorraine Hewitt, Cecilia Rodrigues, Alexandra S Solovyova, Colin R Harwood, Richard J Lewis
Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome.
J Mol Biol: 2012, 416(1);121-36
[PubMed:22198292] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J Bacteriol: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Henrike Pförtner, Leonie Rempeters, Nico Pietack, Christina Herzberg, Jörg Stülke
The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex.
Mol Microbiol: 2010, 77(4);958-71
[PubMed:20572937] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS One: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Stefanie Ehinger, Wolf-Dieter Schubert, Simone Bergmann, Sven Hammerschmidt, Dirk W Heinz
Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites.
J Mol Biol: 2004, 343(4);997-1005
[PubMed:15476816] [WorldCat.org] [DOI] (P 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)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)

C K Brown, P L Kuhlman, S Mattingly, K Slates, P J Calie, W W Farrar
A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis.
J Protein Chem: 1998, 17(8);855-66
[PubMed:9988532] [WorldCat.org] [DOI] (P p)

M A Leyva-Vazquez, P Setlow
Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.
J Bacteriol: 1994, 176(13);3903-10
[PubMed:8021172] [WorldCat.org] [DOI] (P p)

R P Singh, P Setlow
Enolase from spores and cells of Bacillus megaterium: two-step purification of the enzyme and some of its properties.
J Bacteriol: 1978, 134(1);353-5
[PubMed:25885] [WorldCat.org] [DOI] (P p)

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