Abstract:
RRMs are the most common types of RNA recognition modules, being present in about 1% of all human proteins. They adopt a typical βαββαβ fold although N- and C-terminal extensions of these domains have been observed. We have recently characterized the NMR structures of three RRM proteins bound to RNA, in the context of their function in regulating epigenetic (Cyp33), splicing (SRSF1) and translation CPEB (Cytoplasmic polyadenylation element binding protein). For all three RRM containing proteins, the mode of RNA recognition
is very different allowing in each case to propose and explain the mechanism of action of these regulatory factors.