The Dimerization Function of MinC Resides in a Structurally Autonomous C-Terminal Domain
AUTOR(ES)
Szeto, Tim H.
FONTE
American Society for Microbiology
RESUMO
Limited proteolysis of the Escherichia coli cell division inhibitor MinC reveals that its dimerization function resides in a structurally autonomous C-terminal domain. We show that cytoplasmic MinC is poised near the monomer-dimer equilibrium and propose that it only becomes entirely dimeric once recruited to the membrane by MinD.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=95501Documentos Relacionados
- Proteinase inhibitor-inducing activity of the prohormone prosystemin resides exclusively in the C-terminal systemin domain
- The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain.
- Identification of a dimerization domain in the C-terminal segment of the IE110 transactivator protein from herpes simplex virus.
- Structure and function of the C-terminal PABC domain of human poly(A)-binding protein
- Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-5-specific C-terminal domain phosphatases