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Structural features of Argonaute-GW182 protein interactions

Title data

Pfaff, Janina ; Hennig, Janosch ; Herzog, Franz ; Aebersold, Ruedi ; Sattler, Michael ; Niessing, Dierk ; Meister, Gunter:
Structural features of Argonaute-GW182 protein interactions.
In: Proceedings of the National Academy of Sciences of the United States of America. Vol. 110 (2013) Issue 40 . - S. E3770-E3779.
ISSN 1091-6490
DOI: https://doi.org/10.1073/pnas.1308510110

Abstract in another language

MicroRNAs (miRNAs) guide Argonaute (Ago) proteins to target mRNAs, leading to gene silencing. However, Ago proteins are not the actual mediators of gene silencing but interact with a member of the GW182 protein family (also known as GW proteins), which coordinates all downstream steps in gene silencing. GW proteins contain an N-terminal Ago-binding domain that is characterized by multiple GW repeats and a C-terminal silencing domain with several globular domains. Within the Ago-binding domain, Trp residues mediate the direct interaction with the Ago protein. Here, we have characterized the interaction of Ago proteins with GW proteins in molecular detail. Using biochemical and NMR experiments, we show that only a subset of Trp residues engage in Ago interactions. The Trp residues are located in intrinsically disordered regions, where flanking residues mediate additional weak interactions, that might explain the importance of specific tryptophans. Using cross-linking followed by mass spectrometry, we map the GW protein interactions with Ago2, which allows for structural modeling of Ago–GW182 interaction. Our data further indicate that the Ago–GW protein interaction might be a two-step process involving the sequential binding of two tryptophans separated by a spacer with a minimal length of 10 aa.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: RNA interference; RNAi; gene regulation; small RNA–mediated gene silencing
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 08 Oct 2021 06:50
Last Modified: 08 Oct 2021 06:50
URI: https://eref.uni-bayreuth.de/id/eprint/67250