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The structure of human argonaute-2 in complex with miR-20a

Title data

Elkayam, Elad ; Kuhn, Claus-D. ; Tocilj, Ante ; Haase, Astrid D. ; Greene, Emily M. ; Hannon, Gregory J. ; Joshua-Tor, Leemor:
The structure of human argonaute-2 in complex with miR-20a.
In: Cell. Vol. 150 (2012) Issue 1 . - pp. 100-110.
ISSN 0092-8674
DOI: https://doi.org/10.1016/j.cell.2012.05.017

Official URL: Volltext

Abstract in another language

Argonaute proteins lie at the heart of the RNA-induced silencing complex (RISC), wherein they use small RNA guides to recognize targets. Initial insight into the architecture of Argonautes came from studies of prokaryotic proteins, revealing a crescent-shaped base made up of the amino-terminal, PAZ, middle, and PIWI domains. The recently reported crystal structure of human Argonaute-2 (hAgo2), the "slicer" in RNA interference, in complex with a mixed population of RNAs derived from insect cells provides insight into the architecture of a eukaryotic Argonaute protein with defined biochemical and biological functions. Here, we report the structure of human Ago2 bound to a physiologically relevant microRNA, microRNA-20a, at 2.2 A resolution. The miRNA is anchored at both ends by the Mid and PAZ domains and makes several kinks and turns along the binding groove. Interestingly, miRNA binding confers remarkable stability on hAgo2, locking this otherwise flexible enzyme into a stable conformation.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Argonaute Proteins/*chemistry/isolation & purification/*metabolism; Crystallography, X-Ray; Humans; MicroRNAs/*chemistry/*metabolism; Models, Molecular; Protein Structure, Tertiary; Recombinant Proteins/chemistry/isolation & purification/metabolism
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Profile Fields > Advanced Fields > Molecular Biosciences
Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Profile Fields
Profile Fields > Advanced Fields
Research Institutions
Research Institutions > Research Centres
Result of work at the UBT: No
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 10 Jan 2017 10:54
Last Modified: 10 Jan 2017 10:54
URI: https://eref.uni-bayreuth.de/id/eprint/35639