The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression.
The RNA recognition motif (RRM), also known as RNA-binding domain (RBD) or ribonucleoprotein domain (RNP) is one of the most abundant protein domains in eukaryotes. Based on the comparison of more than 40 structures including 15 complexes (RRM-RNA or RRM-protein), we reviewed the structure-function relationships of this domain. We identified and classified the different structural elements of the RRM that are important for binding a multitude of RNA sequences and proteins. Common structural aspects were extracted that allowed us to define a structural leitmotif of the RRM-nucleic acid interface with its variations. Outside of the two conserved RNP motifs that lie in the center of the RRM beta-sheet, the two external beta-strands, the loops, the C- and N-termini, or even a second RRM domain allow high RNA-binding affinity and specific recognition. Protein-RRM interactions that have been found in several structures reinforce the notion of an extreme structural versatility of this domain supporting the numerous biological functions of the RRM-containing proteins.
Maris
Christophe
C
Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology Zurich, ETH-Hönggerberg, Zürich, Switzerland.
Dominguez
Cyril
C
Allain
Frédéric H-T
FH
D000595:Amino Acid Sequence; D005786:Gene Expression Regulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D012313:RNA / Q000378:metabolism; D016415:Sequence Alignment
D012313:RNA