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ATG23, a novel gene required for maturation of proaminopeptidase I, but not for autophagy
ISSN
1567-1364
1567-1356
Date Issued
2004
Author(s)
DOI
10.1016/S1567-1356(03)00207-1
Abstract
In rich media proaminopeptidase I is targeted to the vacuole via the Cvt pathway and during starvation via autophagy. We here identify Atg23 (Y1r431c), a protein of so far unknown function, as a novel component essential for proaminopeptidase I maturation under non-starvation conditions. Maturation of proaminopeptidase I takes place in starved atg23Delta cells. Selective vacuolar targeting of the autophagosomal marker GFP-Aut7 and the accumulation of autophagic bodies during starvation in the presence of phenyltnethylsulfonyl fluoride suggest that autophagy occurs in atg23Delta cells but at a reduced rate. In atg23Delta cells mature vacuolar carboxypeptidase Y is present and accumulation of quinacrine suggests no significant defect in vacuolar acidification. Furthermore, growth of atg23Delta cells on nitrocellulose detects no significant secretion of carboxypeptidase Y. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.