Difference between revisions of "DynA"

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=References=
 
=References=
 +
== Reviews ==
 +
<pubmed> 23109540 20970992 21599493 15040446 </pubmed>
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== Original publications ==
 
<pubmed> 8396117 21205012 20525796 23060960</pubmed>
 
<pubmed> 8396117 21205012 20525796 23060960</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:02, 23 November 2012

  • Description: dynamin-like protein, mediates membrane fusion

Gene name dynA
Synonyms ypbR
Essential no
Product dynamin-like protein
Function fusion of membranes
Gene expression levels in SubtiExpress: dynA
Interactions involving this protein in SubtInteract: DynA
MW, pI 137 kDa, 5.724
Gene length, protein length 3579 bp, 1193 aa
Immediate neighbours ypbS, fbpC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YpbR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DynA expression.png















Categories containing this gene/protein

membrane dynamics, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU22030

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: mediates nucleotide independent membrane fusion in vitro PubMed
  • Protein family: gerABKA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: two separate dynamin-like subunits and GTPase domains PubMed
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Marc Bramkamp
Structure and function of bacterial dynamin-like proteins.
Biol Chem: 2012, 393(11);1203-14
[PubMed:23109540] [WorldCat.org] [DOI] (I p)

Sandra L Schmid, Vadim A Frolov
Dynamin: functional design of a membrane fission catalyst.
Annu Rev Cell Dev Biol: 2011, 27;79-105
[PubMed:21599493] [WorldCat.org] [DOI] (I p)

Harry H Low, Jan Löwe
Dynamin architecture--from monomer to polymer.
Curr Opin Struct Biol: 2010, 20(6);791-8
[PubMed:20970992] [WorldCat.org] [DOI] (I p)

Gerrit J K Praefcke, Harvey T McMahon
The dynamin superfamily: universal membrane tubulation and fission molecules?
Nat Rev Mol Cell Biol: 2004, 5(2);133-47
[PubMed:15040446] [WorldCat.org] [DOI] (P p)

Original publications