Colicin S8 export: extracellular and cytoplasmic colicin are different

Autores/as

  • María-Elena García Díaz Centro de Ingenieria Genética, Facultad de Ciencias, Universidad de los Andes, Mérida, Venezuela
  • Juan Luis Concepción Curbelo Centro de Ingenieria Genética, Facultad de Ciencias, Universidad de los Andes, Mérida, Venezuela

Palabras clave:

Escherichia coli, colicin export, colicin S8, bacteriocins, specific receptors

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.

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Publicado

2010-03-03

Número

Vol. 6 Núm. 4 (2003)

Sección

Research Articles

Licencia

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