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

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Author

  • Michal Letek
  • Maria Fiuza
  • Efren Ordonez
  • Almudena F. Villadangos
  • Klas Flärdh
  • Luis M. Mateos
  • Jose A. Gil

Summary, in English

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.

Publishing year

2009

Language

English

Pages

110-116

Publication/Series

FEMS Microbiology Letters

Volume

297

Issue

1

Document type

Journal article

Publisher

Oxford University Press

Topic

  • Biological Sciences

Keywords

  • swapping domain
  • polar growth
  • DivIVA
  • Corynebacterium
  • cell division
  • two-hybrid system

Status

Published

Research group

  • Microbiology Group

ISBN/ISSN/Other

  • ISSN: 1574-6968