Tethering of the Bacillus subtilis σE proprotein to the cell membrane is necessary for its processing but insufficient for its stabilization

Jingliang Ju, W. G. Haldenwang

Resultado de la investigación: Articlerevisión exhaustiva

6 Citas (Scopus)

Resumen

σE, a sporulation-specific transcription factor of Bacillus subtilis, is synthesized as an inactive proprotein with a 27-amino acid extension at its amino terminus. This "pro" sequence is removed by a developmentally regulated protease, but when present, it blocks σE activity, tethers σE to the bacterium's cytoplasmic membrane, and promotes σE stability. To investigate whether pro-σE processing and/or stabilization are tied to membrane sequestration, we used fluorescent protein fusions to examine the membrane binding of SigE variants. The results are consistent with membrane association as a prerequisite for pro-σE processing but not as a sufficient cause for the proprotein's stability.

Idioma originalEnglish (US)
Páginas (desde-hasta)5897-5900
Número de páginas4
PublicaciónJournal of bacteriology
Volumen185
N.º19
DOI
EstadoPublished - oct. 2003

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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