Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a piwi protein

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Item Type:	Article
Title:	Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a piwi protein
Creators Name:	Simon, B., Kirkpatrick, J.P., Eckhardt, S., Reuter, M., Rocha, E.A., Andrade-Navarro, M.A., Sehr, P., Pillai, R.S. and Carlomagno, T.
Abstract:	Piwi proteins are germline-specific Argonautes that associate with small RNAs called Piwi-interacting RNAs (piRNAs), and together with these RNAs are implicated in transposon silencing. The PAZ domain of Argonaute proteins recognizes the 3'-end of the RNA, which in the case of piRNAs is invariably modified with a 2'-O-methyl group. Here, we present the solution structure of the PAZ domain from the mouse Piwi protein, MIWI, in complex with an 8-mer piRNA mimic. The methyl group is positioned in a hydrophobic cavity made of conserved amino acids from strand β7 and helix α3, where it is contacted by the side chain of methionine-382. Our structure is similar to that of Ago-PAZ, but subtle differences illustrate how the PAZ domain has evolved to accommodate distinct 3' ends from a variety of RNA substrates.
Keywords:	Amino Acid Sequence, Argonaute Proteins, Binding Sites, DNA Transposable Elements, Escherichia coli, Gene Silencing, Molecular Evolution, Methionine, Methylation, Molecular Mimicry, Molecular Sequence Data, Oligonucleotides, Protein Binding, Proteins, Recombinant Proteins, Small Interfering RNA, Surface Plasmon Resonance, Tertiary Protein Structure, Animals, Mice
Source:	Structure
ISSN:	0969-2126
Publisher:	Cell Press
Volume:	19
Number:	2
Page Range:	172-180
Date:	9 February 2011
Official Publication:	https://doi.org/10.1016/j.str.2010.11.015
PubMed:	View item in PubMed

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