000228665 001__ 228665
000228665 005__ 20181203024722.0
000228665 0247_ $$2doi$$a10.15252/embj.201796540
000228665 022__ $$a0261-4189
000228665 02470 $$2ISI$$a000400337600006
000228665 037__ $$aARTICLE
000228665 245__ $$aRae1/YacP, a new endoribonuclease involved in ribosome-dependent mRNA decay in Bacillus subtilis
000228665 260__ $$bWiley$$c2017$$aHoboken
000228665 269__ $$a2017
000228665 300__ $$a15
000228665 336__ $$aJournal Articles
000228665 520__ $$aThe PIN domain plays a central role in cellular RNA biology and is involved in processes as diverse as rRNA maturation, mRNA decay and telomerase function. Here, we solve the crystal structure of the Rae1 (YacP) protein of Bacillus subtilis, a founding member of the NYN (Nedd4-BP1/YacP nuclease) subfamily of PIN domain proteins, and identify potential substrates in vivo. Unexpectedly, degradation of a characterised target mRNA was completely dependent on both its translation and reading frame. We provide evidence that Rae1 associates with the B. subtilis ribosome and cleaves between specific codons of this mRNA in vivo. Critically, we also demonstrate translation-dependent Rae1 cleavage of this substrate in a purified translation assay in vitro. Multiple lines of evidence converge to suggest that Rae1 is an A-site endoribonuclease. We present a docking model of Rae1 bound to the B. subtilis ribosomal A-site that is consistent with this hypothesis and show that Rae1 cleaves optimally immediately upstream of a lysine codon (AAA or AAG) in vivo.
000228665 6531_ $$aA-site ribonuclease
000228665 6531_ $$aBacillus subtilis
000228665 6531_ $$aNYN domain
000228665 6531_ $$aRNA decay
000228665 6531_ $$atranslation
000228665 700__ $$uUniv Paris Diderot, CNRS, Inst Biol Physicochim, Sorbonne Paris Cite,UMR 8261, Paris, France$$aLeroy, Magali
000228665 700__ $$uUniv Paris Diderot, CNRS, Inst Biol Physicochim, Sorbonne Paris Cite,UMR 8261, Paris, France$$aPiton, Jeremie
000228665 700__ $$uUniv Paris Diderot, CNRS, Inst Biol Physicochim, Sorbonne Paris Cite,UMR 8261, Paris, France$$aGilet, Laetitia
000228665 700__ $$uUniv Paris Diderot, CNRS, Inst Biol Physicochim, Sorbonne Paris Cite,UMR 8261, Paris, France$$aPellegrini, Olivier
000228665 700__ $$uInst Pasteur, Ctr Innovat & Technol Res, Transcriptome & EpiGenome Biom, Paris, France$$aProux, Caroline
000228665 700__ $$uInst Pasteur, Ctr Innovat & Technol Res, Transcriptome & EpiGenome Biom, Paris, France$$aCoppee, Jean-Yves
000228665 700__ $$uUniv Paris Diderot, CNRS, Inst Biol Physicochim, Sorbonne Paris Cite,UMR 8261, Paris, France$$aFigaro, Sabine
000228665 700__ $$uUniv Paris Diderot, CNRS, Inst Biol Physicochim, Sorbonne Paris Cite,UMR 8261, Paris, France$$aCondon, Ciaran
000228665 773__ $$j36$$tEmbo Journal$$k9$$q1167-1181
000228665 909C0 $$xU11742$$0252302$$pUPCOL
000228665 909CO $$pSV$$particle$$ooai:infoscience.tind.io:228665
000228665 917Z8 $$x282550
000228665 937__ $$aEPFL-ARTICLE-228665
000228665 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000228665 980__ $$aARTICLE