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 |
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Pages (from-to) | 122-128 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 488 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2017 Jun 17 |
Externally published | Yes |
Keywords
- Hsp70/Sse1 complex
- Nonsense-mediated decay
- Proteasome
- Ubiquitination
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology