Ruedel, Sabine and Wang, Yanli and Lenobel, Rene and Koerner, Roman and Hsiao, He-Hsuan and Urlaub, Henning and Patel, Dinshaw and Meister, Gunter (2011) Phosphorylation of human Argonaute proteins affects small RNA binding. NUCLEIC ACIDS RESEARCH, 39 (6). pp. 2330-2343. ISSN 0305-1048, 1362-4962
Full text not available from this repository. (Request a copy)Abstract
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 whereas Ago 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 human cells. 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SILENCING COMPLEX; AEOLICUS ARGONAUTE; CRYSTAL-STRUCTURE; MESSENGER-RNAS; PIWI-DOMAIN; P-BODIES; MICRORNA; MIRNAS; MECHANISMS; CLEAVAGE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Gunter Meister |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 Jun 2020 09:39 |
| Last Modified: | 25 Jun 2020 09:39 |
| URI: | https://pred.uni-regensburg.de/id/eprint/21247 |
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