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
Sequences	Protein DNA DNA_with_flanks
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)