DivIVA uses an N-terminal conserved region and two coiled-coil domains to localize and sustain the polar growth in Corynebacterium glutamicum

Research output: Contribution to journalArticle

Abstract

Corynebacterium glutamicum is a rod-shaped actinomycete with a distinct model of peptidoglycan synthesis during cell elongation, which takes place at the cell poles and is sustained by the essential protein DivIVA(CG) (C. glutamicum DivIVA). This protein contains a short conserved N-terminal domain and two coiled-coil regions: CC1 and CC2. Domain deletions and chimeric versions of DivIVA were used to functionally characterize the three domains, and all three were found to be essential for proper DivIVA(CG) function. However, in the presence of the N-terminal domain from DivIVA(CG), either of the two coiled-coil domains of DivIVA(CG) could be replaced by the equivalent coiled-coil domain of Bacillus subtilis DivIVA (DivIVA(BS)) without affecting the function of the original DivIVA(CG), and more than one domain had to be exchanged to lose function. Although no single domain was sufficient for subcellular localization or function, CC1 was mainly implicated in stimulating polar growth and CC2 in targeting to DivIVA(CG) assemblies at the cell poles in C. glutamicum.

Details

Authors
  • Michal Letek
  • Maria Fiuza
  • Efren Ordonez
  • Almudena F. Villadangos
  • Klas Flärdh
  • Luis M. Mateos
  • Jose A. Gil
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • swapping domain, polar growth, DivIVA, Corynebacterium, cell division, two-hybrid system
Original languageEnglish
Pages (from-to)110-116
JournalFEMS Microbiology Letters
Volume297
Issue number1
Publication statusPublished - 2009
Publication categoryResearch
Peer-reviewedYes