| Author |
Minami A, Nishi K, Yamada R, Jinnai G, Shima H, Oishi S, Akagawa H, Aono T, Hidaka M, Masaki H, Kuzuyama T, Noda Y, Ogawa T.
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| Abstract |
RNase T2 is a conserved ribonuclease, playing essential and diverse roles despite its simple enzymatic activity. Saccharomyces cerevisiae RNase T2, known as Rny1p, is stress-responsive and localizes in the vacuole. Upon starvation, ribosomes are degraded by autophagy, in which Rny1p mediates rRNA degradation. However, whether the ribosomal degradation is selective or nonselective is still being determined in S. cerevisiae. Here, we elucidated novel aspects of ribosome degradation mechanisms and the function of Rny1p in stress response. We discovered that most ribosomes are selectively degraded, whose mechanism differs from the previously reported selective degradation process called "ribophagy." Rsa1p, a factor involved in assembling 60S ribosomal subunits, is revealed to interact with Atg8p and act as a receptor for selective ribosome degradation in the cytosol. The accumulation of rRNA in vacuoles, due to lack of Rny1p, leads to a decrease in nonselective autophagic activity. This is one of the reasons for the inability of Rny1p-deficient strains to adapt to starvation conditions. Rny1p is also reported to be secreted and associated with the cell wall. We revealed that a C-terminal extension of Rny1p, characteristic in some fungal RNase T2, is required to anchor the cell wall. Some nonfungal RNase T2 proteins also have C-terminal extensions. However, their sequences and structures differ from those of fungal RNase T2, suggesting that their biological functions may also be distinct. The diversity of C-terminal extensions across different organisms is thought to be one reason why RNase T2 plays various roles.
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