Author:
Minami Atsushi,Nishi Kohei,Yamada Rikusui,Jinnai Gai,Shima Hikari,Oishi Sakiko,Akagawa Hirofumi,Aono Toshihiro,Hidaka Makoto,Masaki Haruhiko,Kuzuyama Tomohisa,Noda Yoichi,Ogawa Tetsuhiro
Abstract
ABSTRACTRNase T2 is ubiquitous across diverse organisms, playing essential roles despite its simple enzymatic activity. InSaccharomyces cerevisiae, RNase T2, known as Rny1p, localizes in vacuoles and mediates rRNA degradation during autophagy of ribosomes. In this study, we elucidated novel aspects of ribosome degradation mechanisms and the function of Rny1p. First, we discovered that most ribosomes are degraded by selective autophagy, where Rsa1p is the specific receptor of ribosomes to be degraded. Complex structure prediction suggested that Rsa1p also interacts with Atg8p. Furthermore, we observed that the accumulation of rRNA in vacuoles, due to the lack of Rny1p, leads to a decrease in bulk autophagic activity. This decrease in autophagic activity may explain the inability of Rny1p-deficient strains to adapt to starvation conditions. Second, our structural prediction and biochemical analyses indicate that a C-terminal extension, characteristic in fungal RNase T2 including Rny1p, is not necessary for rRNA degradation but for anchoring to the cell wall. Together with molecular phylogenetic analysis, a species-specific role of RNase T2 conferred by the C-terminal extension is suggested.
Publisher
Cold Spring Harbor Laboratory
Cited by
1 articles.
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