Ribonucleoprotein (RNP)-Partikel Evolution: Vergleichende proteomische und transkriptomische Analyse des Aktin RNP Partikels

16/07/2018 to 14/09/2018

Upon transcription, messenger RNAs (mRNAs) undergo packaging into ribonucleoprotein (RNP) particles composed of multiple RNA-binding proteins (RBPs) and RNA species that are exported from the nucleus. After export into the cytoplasm, messenger RNP (mRNP) particles are remodeled and engage in new RNA- and protein-protein interactions for subsequent targeting to discrete sites within the cell to confer localized mRNA translation. Although individual mRNP particle components are known, the full complement of proteins associated with a single species of mRNA has not been determined. Likewise, it is unclear whether transcripts are packaged alone or with other co-trafficked RNAs. Thus, the minimal composition of an mRNP particle, with respect to the number and species of RBPs and transcripts, is unknown and requires elucidation.

Perhaps the best studied mRNA is that encoding vertebrate ß-actin, one of the most conserved proteins in evolution. Localized translation of ß-actin mRNA controls cell migration or neuronal differentiation and, although a number of RBPs are known to interact with ß-actin mRNA, the nature and structure of the core actin mRNP particle is not known for any organism. The aim of this proposal is to initiate a collaborative study of the core actin mRNP particle in yeast and mammalian cells in order to define common interacting RBPs, transcripts, and structural features for the first time for any mRNP particle. Both the Gerst and Jansen labs focus on RNA trafficking and localized translation using yeast and mammalian cells, and have developed novel techniques for the affinity purification of single transcripts as well as RBP proximity profiling methods, respectively.