| Literature DB >> 21237665 |
Bernd Simon1, John P Kirkpatrick, Stephanie Eckhardt, Michael Reuter, Elsa A Rocha, Miguel A Andrade-Navarro, Peter Sehr, Ramesh S Pillai, Teresa Carlomagno.
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.Entities:
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Year: 2011 PMID： 21237665 DOI： 10.1016/j.str.2010.11.015
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006