Colicin S8 export: extracellular and cytoplasmic colicin are different

• María-Elena García Díaz ^[1] ; Juan Luis Concepción Curbelo ^[1]
  1. [1] Universidad de Los Andes (Venezuela)

     Universidad de Los Andes (Venezuela)

     Venezuela

     
• Localización: International microbiology: official journal of the Spanish Society for Microbiology, ISSN 1139-6709, Vol. 6, Nº. 4, 2003, págs. 263-267
• Idioma: inglés
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• Resumen

  • The properties of colicin S8 are different for the cytoplasmic, periplasmic and extracellular protein. Interactions with its specific receptors reflect this. Active cell extracts separate into a non-anionic along with an anionic fraction by DEAE-Sephacell chromatography. Previously, we have purified cell-associated colicin S8 as an aggregation of highly related polypeptides; cytoplasmic colicin S8 seems to be post-translationally processed into an aggregation of polypeptides of molecular mass ranging from 45,000 Da to 60,000 Da. We suggest that a conformational change to colicin S8 may occur related to the export process.