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RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis.

Authors :
Lange, Heike
Ndecky, Simon Y. A.
Gomez-Diaz, Carlos
Pflieger, David
Butel, Nicolas
Zumsteg, Julie
Kuhn, Lauriane
Piermaria, Christina
Chicher, Johana
Christie, Michael
Karaaslan, Ezgi S.
Lang, Patricia L. M.
Weigel, Detlef
Vaucheret, Hervé
Hammann, Philippe
Gagliardi, Dominique
Source :
Nature Communications; 8/27/2019, Vol. 10 Issue 1, pN.PAG-N.PAG, 1p
Publication Year :
2019

Abstract

The RNA exosome is a key 3'−5' exoribonuclease with an evolutionarily conserved structure and function. Its cytosolic functions require the co-factors SKI7 and the Ski complex. Here we demonstrate by co-purification experiments that the ARM-repeat protein RESURRECTION1 (RST1) and RST1 INTERACTING PROTEIN (RIPR) connect the cytosolic Arabidopsis RNA exosome to the Ski complex. rst1 and ripr mutants accumulate RNA quality control siRNAs (rqc-siRNAs) produced by the post-transcriptional gene silencing (PTGS) machinery when mRNA degradation is compromised. The small RNA populations observed in rst1 and ripr mutants are also detected in mutants lacking the RRP45B/CER7 core exosome subunit. Thus, molecular and genetic evidence supports a physical and functional link between RST1, RIPR and the RNA exosome. Our data reveal the existence of additional cytosolic exosome co-factors besides the known Ski subunits. RST1 is not restricted to plants, as homologues with a similar domain architecture but unknown function exist in animals, including humans. Cytosolic RNA degradation by the RNA exosome requires the Ski complex. Here the authors show that the proteins RST1 and RIPR assist the RNA exosome and the Ski complex in RNA degradation, thereby preventing the production of secondary siRNAs from endogenous mRNAs. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
20411723
Volume :
10
Issue :
1
Database :
Complementary Index
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
138298313
Full Text :
https://doi.org/10.1038/s41467-019-11807-4