Phosphorylation of human Argonaute proteins affects small RNA binding

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F11%3A33148777" target="_blank" >RIV/61989592:15310/11:33148777 - isvavai.cz</a>
Result on the web
<a href="http://nar.oxfordjournals.org/content/39/6/2330" target="_blank" >http://nar.oxfordjournals.org/content/39/6/2330</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkq1032" target="_blank" >10.1093/nar/gkq1032</a>

Result language
angličtina
Original language name
Phosphorylation of human Argonaute proteins affects small RNA binding
Original language description
Argonaute (Ago) proteins are highly conserved between species and constitute a direct-binding platform for small RNAs including short-interfering RNAs (siRNAs), microRNAs (miRNAs) and Piwi interacting RNAs (piRNAs). Small RNAs function as guides whereasAgo proteins are the actual mediators of gene silencing. Although the major steps in RNA-guided gene silencing have been elucidated, not much is known about Ago-protein regulation. Here we report a comprehensive analysis of Ago2 phosphorylation in humancells. We find that the highly conserved tyrosine Y529, located in the small RNA 5'-end-binding pocket of Ago proteins can be phosphorylated. By substituting Y529 with a negatively charged glutamate (E) mimicking a phosphorylated tyrosine, we show that small RNA binding is strongly reduced. Our data suggest that a negatively charged phospho-tyrosine generates a repulsive force that prevents efficient binding of the negatively charged 5' phosphate of the small RNA
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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