Degradation of SERRATE via ubiquitin-independent 20S proteasome to survey RNA metabolism.

Nature Plants
Yanjun LiXiuren Zhang

Abstract

SERRATE (SE) is a key factor in RNA metabolism. Here, we report that SE binds 20S core proteasome α subunit G1 (PAG1) among other components and is accumulated in their mutants. Purified PAG1-containing 20S proteasome degrades recombinant SE via an ATP- and ubiquitin-independent manner in vitro. Nevertheless, PAG1 is a positive regulator for SE in vivo, as pag1 shows comparable molecular and/or developmental defects relative to se. Furthermore, SE is poorly assembled into macromolecular complexes, exemplified by the microprocessor in pag1 compared with Col-0. SE overexpression triggered the destruction of both transgenic and endogenous protein, leading to similar phenotypes of se and SE overexpression lines. We therefore propose that PAG1 degrades the intrinsically disordered portion of SE to secure the functionality of folded SE that is assembled and protected in macromolecular complexes. This study provides insight into how the 20S proteasome regulates RNA metabolism through controlling its key factor in eukaryotes.

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Citations

Feb 12, 2021·Plant Science : an International Journal of Experimental Plant Biology·Jinjin LiHaiyan Zhang
Jan 24, 2021·Journal of Experimental Botany·Jiaying ZhuXiuren Zhang
Apr 30, 2021·Science Advances·Qi LiXiaoming Zhang

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Methods Mentioned

BETA
transgenic
co-immunoprecipitation
Y2H
PCR
RNA-seq
ubiquitination
confocal microscopy
transfection
fluorescence resonance
Co-IP

Software Mentioned

FoldIndex

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