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Article Dans Une Revue Journal of Bacteriology Année : 2002

Membrane topology of the Streptococcus pneumoniae FtsW division protein

Résumé

The topology of FtsW from Streptococcus pneumoniae, an essential membrane protein involved in bacterial cell division, was predicted by computational methods and probed by the alkaline phosphatase fusion and cysteine accessibility techniques. Consistent results were obtained for the seven N-terminal membrane-spanning segments. However, the results from alkaline phosphatase fusions did not confirm the hydropathy analysis of the C-terminal part of FtsW, whereas the accessibility of introduced cysteine residues was in agreement with the theoretical prediction. Based on the combined results, we propose the first topological model of FtsW, featuring 10 membrane-spanning segments, a large extracytoplasmic loop, and both N and C termini located in the cytoplasm.
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Dates et versions

hal-01601049 , version 1 (02-10-2017)

Identifiants

  • HAL Id : hal-01601049 , version 1
  • PRODINRA : 383048
  • PUBMED : 11889099
  • WOS : 000174454000016

Citer

Philippe Gerard, Thierry Vernet, André Zapun. Membrane topology of the Streptococcus pneumoniae FtsW division protein. Journal of Bacteriology, 2002, 184 (7), pp.1925-1931. ⟨hal-01601049⟩
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