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1.
  • Letek, Michal, et al. (författare)
  • DivIVA is required for polar growth in the MreB-lacking rod-shaped actinomycete Corynebacterium glutamicum.
  • 2008
  • Ingår i: Journal of Bacteriology. - 0021-9193. ; 190, s. 3283-3292
  • Tidskriftsartikel (refereegranskat)abstract
    • The actinomycete Corynebacterium glutamicum grows as rod-shaped cells by zonal peptidoglycan synthesis at the cell poles. In this bacterium, experimental depletion of the polar DivIVACG protein resulted in the inhibition of polar growth; consequently, these cells exhibited a coccoid morphology. This result demonstrated that DivIVA is required for cell elongation and the acquisition of a rod shape. DivIVA from Streptomyces or Mycobacterium localized to the cell poles of DivIVACG-depleted C. glutamicum and restored polar peptidoglycan synthesis, in contrast to DivIVAs from Bacillus subtilis or Streptococcus pneumoniae which localized at the septum of C. glutamicum. This confirmed that DivIVAs from actinomycetes are involved in polarized cell growth. DivIVACG localized at the septum after cell-wall synthesis had started and the nucleoids had already segregated, suggesting that in C. glutamicum DivIVA is not involved in cell division or chromosome segregation.
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2.
  • Letek, Michal, et al. (författare)
  • DivIVA uses an N-terminal conserved region and two coiled-coil domains to localize and sustain the polar growth in Corynebacterium glutamicum
  • 2009
  • Ingår i: FEMS Microbiology Letters. - : Oxford University Press (OUP). - 1574-6968 .- 0378-1097. ; 297:1, s. 110-116
  • Tidskriftsartikel (refereegranskat)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.
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  • Resultat 1-2 av 2
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Flärdh, Klas (2)
Letek, Michal (2)
Gil, Jose A. (2)
Ordóñez, Efrén (2)
Mateos, Luis M (2)
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