5MQ9

Crystal structure of Rae1 (YacP) from Bacillus subtilis (W164L mutant)

Summary for 5MQ9

• Entry DOI: 10.2210/pdb5mq9/pdb
• Descriptor: Uncharacterized protein YacP, SULFATE ION (3 entities in total)
• Functional Keywords: b. subtilis, rna maturation and decay, endonuclease, translation, peptide toxin
• Biological source: Bacillus subtilis subsp. subtilis str. 168
• Total number of polymer chains: 2
• Total formula weight: 42117.83

Authors

Piton, J.,Gilet, L.,Pellegrini, O.,Leroy, M.,Figaro, S.,Condon, C. (deposition date: 2016-12-20, release date: 2017-04-19, Last modification date: 2024-05-08)

Primary citation

Leroy, M.,Piton, J.,Gilet, L.,Pellegrini, O.,Proux, C.,Coppee, J.Y.,Figaro, S.,Condon, C.
Rae1/YacP, a new endoribonuclease involved in ribosome-dependent mRNA decay in Bacillus subtilis.
EMBO J., 36:1167-1181, 2017

PubMed Abstract: The 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 , a founding member of the NYN (Nedd4-BP1/YacP nuclease) subfamily of PIN domain proteins, and identify potential substrates 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 ribosome and cleaves between specific codons of this mRNA Critically, we also demonstrate translation-dependent Rae1 cleavage of this substrate in a purified translation assay Multiple lines of evidence converge to suggest that Rae1 is an A-site endoribonuclease. We present a docking model of Rae1 bound to the ribosomal A-site that is consistent with this hypothesis and show that Rae1 cleaves optimally immediately upstream of a lysine codon (AAA or AAG) .

PubMed: 28363943
DOI: 10.15252/embj.201796540

Experimental method

X-RAY DIFFRACTION (3.174 Å)