Processing of yeast exoglucanase (beta-glucosidase) in a KEX2-dependent manner.
We have detected proteolytic processing of a form of exoglucanase representative of the endoplasmic reticulum (form A). This processing did not take place when form A was obtained from protoplasts lysed in the presence of either EDTA or leupeptin, two wel-characterized inhibitors of KEX2 endoprotease from Saccharomyces cerevisiae. Sequencing of the amino terminus of an A-like form of enzyme secreted by a kex2 mutant indicated the presence of 4 amino acids, with a pair of basic residues (Lys-Arg) at their carboxyl side, preceding the amino terminus of the wild-type external exoglucanase.
Basco
R D
RD
Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
Giménez-Gallego
G
G
Larriba
G
G
D000595:Amino Acid Sequence; D015153:Blotting, Western; D043326:Glucan 1,3-beta-Glucosidase; D005959:Glucosidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D043484:Proprotein Convertases; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000378:metabolism*; D013381:Subtilisins; D001617:beta-Glucosidase / Q000378:metabolism*
D029701:Saccharomyces cerevisiae Proteins; D005959:Glucosidases; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase; D043484:Proprotein Convertases; D012697:Serine Endopeptidases; D013381:Subtilisins; C058751:KEX2 protein, S cerevisiae