Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product

Takato Sugiyama; Risa Nobuta; Koji Ando; Yasuko Matsuki; Toshifumi Inada

doi:10.1016/j.bbrc.2017.05.020

Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product

Takato Sugiyama, Risa Nobuta, Koji Ando, Yasuko Matsuki, Toshifumi Inada

PHA - Life and Pharmaceutical Science

Research output: Contribution to journal › Article

1 Citation (Scopus)

Abstract

Up-frameshift (Upf) complex facilitates the degradation of aberrant mRNAs containing a premature termination codon (PTC) and its products in yeast. Here we report that Sse1, a member of the Hsp110 family, and Hsp70 play a crucial role in Upf-dependent degradation of the truncated FLAG-Pgk1-300 protein derived from PGK1 mRNA harboring a PTC at codon position 300. Sse1 was required for Upf-dependent rapid degradation of the FLAG-Pgk1-300. FLAG-Pgk1-300 was significantly destabilized in ATP hydrolysis defective sse1-1 mutant cells than in wild type cells. Consistently, Sse1 and Hsp70 reduced the level of an insoluble form of FLAG-Pgk1-300. We propose that the Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes.

Original language	English
Pages (from-to)	122-128
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	488
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2017.05.020
Publication status	Published - 2017 Jun 17

Keywords

Hsp70/Sse1 complex
Nonsense-mediated decay
Proteasome
Ubiquitination

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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Sugiyama, T., Nobuta, R., Ando, K., Matsuki, Y., & Inada, T. (2017). Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product. Biochemical and Biophysical Research Communications, 488(1), 122-128. https://doi.org/10.1016/j.bbrc.2017.05.020

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abstract = "Up-frameshift (Upf) complex facilitates the degradation of aberrant mRNAs containing a premature termination codon (PTC) and its products in yeast. Here we report that Sse1, a member of the Hsp110 family, and Hsp70 play a crucial role in Upf-dependent degradation of the truncated FLAG-Pgk1-300 protein derived from PGK1 mRNA harboring a PTC at codon position 300. Sse1 was required for Upf-dependent rapid degradation of the FLAG-Pgk1-300. FLAG-Pgk1-300 was significantly destabilized in ATP hydrolysis defective sse1-1 mutant cells than in wild type cells. Consistently, Sse1 and Hsp70 reduced the level of an insoluble form of FLAG-Pgk1-300. We propose that the Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes.",

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AU - Sugiyama, Takato

AU - Nobuta, Risa

AU - Ando, Koji

AU - Matsuki, Yasuko

AU - Inada, Toshifumi

PY - 2017/6/17

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N2 - Up-frameshift (Upf) complex facilitates the degradation of aberrant mRNAs containing a premature termination codon (PTC) and its products in yeast. Here we report that Sse1, a member of the Hsp110 family, and Hsp70 play a crucial role in Upf-dependent degradation of the truncated FLAG-Pgk1-300 protein derived from PGK1 mRNA harboring a PTC at codon position 300. Sse1 was required for Upf-dependent rapid degradation of the FLAG-Pgk1-300. FLAG-Pgk1-300 was significantly destabilized in ATP hydrolysis defective sse1-1 mutant cells than in wild type cells. Consistently, Sse1 and Hsp70 reduced the level of an insoluble form of FLAG-Pgk1-300. We propose that the Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes.

AB - Up-frameshift (Upf) complex facilitates the degradation of aberrant mRNAs containing a premature termination codon (PTC) and its products in yeast. Here we report that Sse1, a member of the Hsp110 family, and Hsp70 play a crucial role in Upf-dependent degradation of the truncated FLAG-Pgk1-300 protein derived from PGK1 mRNA harboring a PTC at codon position 300. Sse1 was required for Upf-dependent rapid degradation of the FLAG-Pgk1-300. FLAG-Pgk1-300 was significantly destabilized in ATP hydrolysis defective sse1-1 mutant cells than in wild type cells. Consistently, Sse1 and Hsp70 reduced the level of an insoluble form of FLAG-Pgk1-300. We propose that the Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes.

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