Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus

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Abstract

tRNAs are unique among various RNAs in that they shuttle between the nucleus and the cytoplasm, and their localization is regulated by nutrient conditions. Although nuclear export of tRNAs has been well documented, the import machinery is poorly understood. Here, we identified Ssa2p, a major cytoplasmic Hsp70 in Saccharomyces cerevisiae, as a tRNA-binding protein whose deletion compromises nuclear accumulation of tRNAs upon nutrient starvation. Ssa2p recognizes several structural features of tRNAs through its nucleotide-binding domain, but prefers loosely-folded tRNAs, suggesting that Ssa2p has a chaperone-like activity for RNAs. Ssa2p also binds Nup116, one of the yeast nucleoporins. Sis1p and Ydj1p, cytoplasmic co-chaperones for Ssa proteins, were also found to contribute to the tRNA import. These results unveil a novel function of the Ssa2p system as a tRNA carrier for nuclear import by a novel mode of substrate recognition. Such Ssa2p-mediated tRNA import likely contributes to quality control of cytosolic tRNAs.

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Akira Takano

Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya, Japan

Competing interests
The authors declare that no competing interests exist.
Takuya Kajita

Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya, Japan

Competing interests
The authors declare that no competing interests exist.
Makoto Mochizuki

Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya, Japan

Competing interests
The authors declare that no competing interests exist.
Toshiya Endo

Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya, Japan

Competing interests
The authors declare that no competing interests exist.
Tohru Yoshihisa

Graduate School of Life Science, University of Hyogo, Kobe, Japan

For correspondence
tyoshihi@sci.u-hyogo.ac.jp

Competing interests
The authors declare that no competing interests exist.

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