DynA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, cell shape, membrane dynamics, membrane proteins

The gene

Basic information

• Locus tag: BSU22030

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Cofactor(s): Mg(2+) PubMed

• Effectors of protein activity:

• Interactions:
  • forms oligomers PubMed
  • DynA-RNase Y PubMed
  • DynA-YneK PubMed
  • DynA-YwpG PubMed

• Localization:
  • associated to the membrane PubMed
  • membrane, forms foci at the site of septation PubMed
  • colocalizes with FtsZ PubMed

Database entries

• Structure:

• UniProt: P54159

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: dynA PubMed

• Expression browser: dynA PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

Felix Dempwolff, Hanna M Wischhusen, Mara Specht, Peter L Graumann
The deletion of bacterial dynamin and flotillin genes results in pleiotrophic effects on cell division, cell growth and in cell shape maintenance.
BMC Microbiol: 2012, 12;298
[PubMed:23249255] [WorldCat.org] [DOI] (I e)

Frank Bürmann, Prachi Sawant, Marc Bramkamp
Identification of interaction partners of the dynamin-like protein DynA from Bacillus subtilis.
Commun Integr Biol: 2012, 5(4);362-9
[PubMed:23060960] [WorldCat.org] [DOI] (I p)

Frank Bürmann, Nina Ebert, Suey van Baarle, Marc Bramkamp
A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion.
Mol Microbiol: 2011, 79(5);1294-304
[PubMed:21205012] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

L Chen, L P James, J D Helmann
Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions.
J Bacteriol: 1993, 175(17);5428-37
[PubMed:8396117] [WorldCat.org] [DOI] (P p)