Project Details
Projekt
beta-propeller domains as novel RNA-binding modules
Applicant
Professor Dr. Gunter Meister
Subject Area
General Genetics and Functional Genome Biology
Biochemistry
Biochemistry
Term
from 2016 to 2023
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 313644909
All cellular RNAs are embedded into RNA-protein complexes and form dynamic RNPs to facilitate their various functions. This is not only true for well-characterized non-coding RNPs such as ribosomes of small nuclear RNPs (snRNPs), but also for mRNAs, which are incorporated into mRNPs. Already during transcription, dynamic pre-mRNPs form that are subsequently remodeled until they reach ribosomes for translation. Besides the RNA itself, RNA binding proteins (RBPs) are central factors within RNPs. This large and diverse protein family can, for example, serve as scaffold or contribute enzymatic activity to RNPs. RBPs directly contact the RNA and therefore contain specialized domains or motifs, which are referred to as RNA binding domains (RBDs). Although thousands of RBPs exist, only a rather small number of RBDs have been characterized. Unlike DNA binding domains, which often interact with the major or the minor groove of double stranded DNA, many single stranded RBDs interact with individual bases and thus contact highly specific RNA motifs.We identified and characterized the NHL (NCL-1, HT2A, Lin41) domain as novel RBD. It is composed of a so-called β-propeller fold, in which several β-sheets (‘blades’) are organized in a ‘propeller’-like structure. Sequence-specific RNA recognition is achieved by distinct contacts of RNA bases with amino acid residues located in the clefts between the blades of the β-propeller. WD40 domains are also composed of β-propeller structures. WD40 domains are among the most abundant protein domains and therefore, we reasoned that some of these domains might also contain RNA binding activity. This hypothesis forms the basis of our project proposal and we hope that we can contribute insights into the various ways of protein-RNA interaction.
DFG Programme
Priority Programmes
