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Structural features of Argonaute-GW182 protein interactions

Titelangaben

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. Bd. 110 (2013) Heft 40 . - S. E3770-E3779.
ISSN 1091-6490
DOI: https://doi.org/10.1073/pnas.1308510110

Abstract

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.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: RNA interference; RNAi; gene regulation; small RNA–mediated gene silencing
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie mit Schwerpunkt Biophysikalische Chemie > Lehrstuhl Biochemie mit Schwerpunkt Biophysikalische Chemie - Univ.-Prof. Dr. Janosch Hennig
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie mit Schwerpunkt Biophysikalische Chemie
Titel an der UBT entstanden: Nein
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 540 Chemie
500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 08 Okt 2021 06:50
Letzte Änderung: 08 Okt 2021 06:50
URI: https://eref.uni-bayreuth.de/id/eprint/67250