Dueck, Anne and Ziegler, Christian and Eichner, Alexander and Berezikov, Eugene and Meister, Gunter (2012) microRNAs associated with the different human Argonaute proteins. NUCLEIC ACIDS RESEARCH, 40 (19). pp. 9850-9862. ISSN 0305-1048,
Full text not available from this repository. (Request a copy)Abstract
MicroRNAs (miRNAs) are small noncoding RNAs that function in literally all cellular processes. miRNAs interact with Argonaute (Ago) proteins and guide them to specific target sites located in the 3'-untranslated region (3'-UTR) of target mRNAs leading to translational repression and deadenylation-induced mRNA degradation. Most miRNAs are processed from hairpin-structured precursors by the consecutive action of the RNase III enzymes Drosha and Dicer. However, processing of miR-451 is Dicer independent and cleavage is mediated by the endonuclease Ago2. Here we have characterized miR-451 sequence and structure requirements for processing as well as sorting of miRNAs into different Ago proteins. Pre-miR-451 appears to be optimized for Ago2 cleavage and changes result in reduced processing. In addition, we show that the mature miR-451 only associates with Ago2 suggesting that mature miRNAs are not exchanged between different members of the Ago protein family. Based on cloning and deep sequencing of endogenous miRNAs associated with Ago1-3, we do not find evidence for miRNA sorting in human cells. However, Ago identity appears to influence the length of some miRNAs, while others remain unaffected.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MESSENGER-RNA TRANSLATION; PASSENGER-STRAND; SIRNA; IDENTIFICATION; BIOGENESIS; MECHANISMS; DROSOPHILA; COMPLEXES; CLEAVAGE; CELLS; |
| 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: | 05 May 2020 05:25 |
| Last Modified: | 05 May 2020 05:25 |
| URI: | https://pred.uni-regensburg.de/id/eprint/18009 |
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