Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE RESEARCH
DOI: 10.1038/ncomms11846
Keywords
-
Categories
Funding
- JSPS KAKENHI [25840019, 16K07246]
- Takeda Science Foundation
- Naito Foundation
- Sasaki Environment Technology Foundation
- Union Tool Scholarship Foundation
- Grants-in-Aid for Scientific Research [16K07246, 25840019] Funding Source: KAKEN
Ask authors/readers for more resources
Argonaute proteins are key players in the gene silencing mechanisms mediated by small nucleic acids in all domains of life from bacteria to eukaryotes. However, little is known about the Argonaute protein that recognizes guide RNA/target DNA. Here, we determine the 2 angstrom crystal structure of Rhodobacter sphaeroides Argonaute (RsAgo) in a complex with 18-nucleotide guide RNA and its complementary target DNA. The heteroduplex maintains Watson-Crick base-pairing even in the 30-region of the guide RNA between the N-terminal and PIWI domains, suggesting a recognition mode by RsAgo for stable interaction with the target strand. In addition, the MID/PIWI interface of RsAgo has a system that specifically recognizes the 50 base-U of the guide RNA, and the duplex-recognition loop of the PAZ domain is important for the DNA silencing activity. Furthermore, we show that Argonaute discriminates the nucleic acid type (RNA/DNA) by recognition of the duplex structure of the seed region.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available