Hauptmann, Judith and Kater, Lukas and Loeffler, Patrick and Merkl, Rainer and Meister, Gunter (2014) Generation of catalytic human Ago4 identifies structural elements important for RNA cleavage. RNA, 20 (10). pp. 1532-1538. ISSN 1355-8382, 1469-9001
Full text not available from this repository. (Request a copy)Abstract
Argonaute proteins bind small RNAs and mediate cleavage of complementary target RNAs. The human Argonaute protein Ago4 is catalytically inactive, although it is highly similar to catalytic Ago2. Here, we have generated Ago2-Ago4 chimeras and analyzed their cleavage activity in vitro. We identify several specific features that inactivate Ago4: the catalytic center, short sequence elements in the N-terminal domain, and an Ago4-specific insertion in the catalytic domain. In addition, we show that Ago2-mediated cleavage of the noncanonical miR-451 precursor can be carried out by any catalytic human Ago protein. Finally, phylogenetic analyses establish evolutionary distances between the Ago proteins. Interestingly, these distances do not fully correlate with the structural changes inactivating them, suggesting functional adaptations of individual human Ago proteins.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HUMAN ARGONAUTE PROTEINS; CRYSTAL-STRUCTURE; RECOGNITION; DOMAIN; INSIGHTS; REVEALS; PATHWAY; BINDING; Argonaute proteins; Ago4; microRNAs; RNAi; siRNAs; gene silencing |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Rainer Merkl Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Gunter Meister |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 13 Aug 2019 09:43 |
| Last Modified: | 13 Aug 2019 09:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/9504 |
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