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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/H2J4R4_MARPK H2J4R4_MARPK] | | [https://www.uniprot.org/uniprot/H2J4R4_MARPK H2J4R4_MARPK] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Eukaryotic Argonaute proteins induce gene silencing by small RNA-guided recognition and cleavage of mRNA targets. Although structural similarities between human and prokaryotic Argonautes are consistent with shared mechanistic properties, sequence and structure-based alignments suggested that Argonautes encoded within CRISPR-cas[clustered regularly interspaced short palindromic repeats (CRISPR)-associated] bacterial immunity operons have divergent activities. We show here that the CRISPR-associatedMarinitoga piezophilaArgonaute (MpAgo) protein cleaves single-stranded target sequences using 5'-hydroxylated guide RNAs rather than the 5'-phosphorylated guides used by all known Argonautes. The 2.0-A resolution crystal structure of an MpAgo-RNA complex reveals a guide strand binding site comprising residues that block 5' phosphate interactions. Using structure-based sequence alignment, we were able to identify other putative MpAgo-like proteins, all of which are encoded within CRISPR-casloci. Taken together, our data suggest the evolution of an Argonaute subclass with noncanonical specificity for a 5'-hydroxylated guide.
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| A bacterial Argonaute with noncanonical guide RNA specificity.,Kaya E, Doxzen KW, Knoll KR, Wilson RC, Strutt SC, Kranzusch PJ, Doudna JA Proc Natl Acad Sci U S A. 2016 Mar 30. pii: 201524385. PMID:27035975<ref>PMID:27035975</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5i4a" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Argonaute 3D structures|Argonaute 3D structures]] | | *[[Argonaute 3D structures|Argonaute 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
