Journal Article

<i>ATG23</i>, a novel gene required for maturation of proaminopeptidase I, but not for autophagy

Khuyen Meiling-Wesse, Fotini Bratsika and Michael Thumm

in FEMS Yeast Research

Volume 4, issue 4-5, pages 459-465
Published in print January 2004 |
Published online January 2006 | e-ISSN: 1567-1364 | DOI:

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In rich media proaminopeptidase I is targeted to the vacuole via the Cvt pathway and during starvation via autophagy. We here identify Atg23 (Ylr431c), 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 atg23Δ cells. Selective vacuolar targeting of the autophagosomal marker GFP-Aut7 and the accumulation of autophagic bodies during starvation in the presence of phenylmethylsulfonyl fluoride suggest that autophagy occurs in atg23Δ cells but at a reduced rate. In atg23Δ cells mature vacuolar carboxypeptidase Y is present and accumulation of quinacrine suggests no significant defect in vacuolar acidification. Furthermore, growth of atg23Δ cells on nitrocellulose detects no significant secretion of carboxypeptidase Y.

Keywords: Autophagy; Cvt pathway; Maturation of proaminopeptidase I; Yeast deletion strain collection

Journal Article.  3445 words.  Illustrated.

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