Colicin S8 export: extracellular and cytoplasmic colicin are different.
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.
Garcia Diaz
Maria-Elena
ME
Centro de Ingenieria Genética, Facultad de Ciencias, Universidad de los Andes, Ruta 5853, La Hechicera 510, ZP.9995-P, Mérida, Venezuela. malena03@cantv.net
Concepción Curbelo
Juan Luis
JL
D002852:Chromatography, Ion Exchange; D003087:Colicins / Q000302:isolation & purification / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D005110:Extracellular Space / Q000378:metabolism; D021381:Protein Transport
D003087:Colicins; D029968:Escherichia coli Proteins; C483612:colicin S8, E coli