The SmAP1/2 proteins of the crenarchaeon Sulfolobus solfataricus interact with the exosome and stimulate A-rich tailing of transcripts

Nucleic Acids Research
Birgit MärtensUdo Bläsi

Abstract

The conserved Sm and Sm-like proteins are involved in different aspects of RNA metabolism. Here, we explored the interactome of SmAP1 and SmAP2 of the crenarchaeon Sulfolobus solfataricus (Sso) to shed light on their physiological function(s). Both, SmAP1 and SmAP2 co-purified with several proteins involved in RNA-processing/modification, translation and protein turnover as well as with components of the exosome involved in 3΄ to 5΄ degradation of RNA. In follow-up studies a direct interaction with the poly(A) binding and accessory exosomal subunit DnaG was demonstrated. Moreover, elevated levels of both SmAPs resulted in increased abundance of the soluble exosome fraction, suggesting that they affect the subcellular localization of the exosome in the cell. The increased solubility of the exosome was accompanied by augmented levels of RNAs with A-rich tails that were further characterized using RNASeq. Hence, the observation that the Sso SmAPs impact on the activity of the exosome revealed a hitherto unrecognized function of SmAPs in archaea.

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Citations

Sep 13, 2018·Annual Review of Genetics·José Vicente Gomes-FilhoLennart Randau
Apr 18, 2019·Annals of the New York Academy of Sciences·José Vicente Gomes-Filho, Lennart Randau
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Apr 9, 2021·Biochemistry. Biokhimii︠a︡·Natalia V LekontsevaAlexey D Nikulin

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Datasets Mentioned

BETA
PRJEB20182

Methods Mentioned

BETA
Co-IP
affinity purification
affinity purifications
affinity-purifications
GTPase
size-exclusion chromatography
pull-down
Co-immunoprecipitation
RNA Seq
protein folding

Software Mentioned

Proteome
Mascot
WebLogo
ViennaNGS
BEDtools
Scaffold

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