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Nat Struct Mol Biol. 2014 Sep;21(9):743-53. doi: 10.1038/nsmb.2879.

The evolutionary journey of Argonaute proteins.

Author information

1
Laboratory of Microbiology, Department of Agrotechnology and Food Sciences, Wageningen University, Wageningen, the Netherlands.
2
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, USA.
3
Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
4
Department of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio, USA.
5
Institute for Molecular Biology, Mainz, Germany.
6
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.

Abstract

Argonaute proteins are conserved throughout all domains of life. Recently characterized prokaryotic Argonaute proteins (pAgos) participate in host defense by DNA interference, whereas eukaryotic Argonaute proteins (eAgos) control a wide range of processes by RNA interference. Here we review molecular mechanisms of guide and target binding by Argonaute proteins, and describe how the conformational changes induced by target binding lead to target cleavage. On the basis of structural comparisons and phylogenetic analyses of pAgos and eAgos, we reconstruct the evolutionary journey of the Argonaute proteins through the three domains of life and discuss how different structural features of pAgos and eAgos relate to their distinct physiological roles.

PMID:
25192263
PMCID:
PMC4691850
DOI:
10.1038/nsmb.2879
[Indexed for MEDLINE]
Free PMC Article

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