Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod. - Groupe Pneumocoque / Pneumococcus Group (IBS-PG) Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 2009

Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod.

Thomas Kern
  • Fonction : Auteur
Audrey Le Gouellec
Jean-Pierre Simorre
Philip Callow
  • Fonction : Auteur
Thierry Vernet
André Zapun

Résumé

DivIB(FtsQ), FtsL, and DivIC(FtsB) are enigmatic membrane proteins that are central to the process of bacterial cell division. DivIB(FtsQ) is dispensable in specific conditions in some species, and appears to be absent in other bacterial species. The presence of FtsL and DivIC(FtsB) appears to be conserved despite very low sequence conservation. The three proteins form a complex at the division site, FtsL and DivIC(FtsB) being associated through their extracellular coiled-coil region. We report here structural investigations by NMR, small-angle neutron and x-ray scattering, and interaction studies by surface plasmon resonance, of the complex of DivIB, FtsL, and DivIC from Streptococcus pneumoniae, using soluble truncated forms of the proteins. We found that one side of the "bean"-shaped central beta-domain of DivIB interacts with the C-terminal regions of the dimer of FtsL and DivIC. This finding is corroborated by sequence comparisons across bacterial genomes. Indeed, DivIB is absent from species with shorter FtsL and DivIC proteins that have an extracellular domain consisting only of the coiled-coil segment without C-terminal conserved regions (Campylobacterales). We propose that the main role of the interaction of DivIB with FtsL and DivIC is to help the formation, or to stabilize, the coiled-coil of the latter proteins. The coiled-coil of FtsL and DivIC, itself or with transmembrane regions, could be free to interact with other partners.
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Dates et versions

hal-01464089 , version 1 (09-02-2017)

Identifiants

  • HAL Id : hal-01464089 , version 1
  • PUBMED : 19635793

Citer

Soizic Masson, Thomas Kern, Audrey Le Gouellec, Cécile Giustini, Jean-Pierre Simorre, et al.. Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod.. Journal of Biological Chemistry, 2009, pp.27687-700. ⟨hal-01464089⟩
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