Strukturelle Basis der Polyadenylierung zytoplasmatischer Boten-RNA durch den GLD-2/GLD-3 Proteinkomplex

• Antragstellerin: Dr. Katharina Nakel
• Fachliche Zuordnung: Strukturbiologie
• Förderung: Förderung von 2008 bis 2016
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 96970106

Polyadenylation of messenger RNA is an essential process in eukaryotes. In the nucleus it influences mRNA stability and transport, while in the cytoplasm it impacts on mRNA translational efficiency. Cytoplasmic polyadenylation is essential for a variety of cellular processes. Dormant cytoplasmic mRNAs of maternal origin, for example, are activated for protein synthesis at specific times during oocyte maturation and early development by addition of a poly(A) tail. Polyadenylation is carried out by poly(A) polymerases (PAPs), proteins of the nucleotidyl-transferase family whose catalytic core domain is highly conserved across species. In contrast to nuclear PAPs, cytoplasmic PAPs are activated by and act in conjunction with other proteins. The structural basis for their function is currently unknown. I plan to characterize the X-ray structure of the cytoplasmic poly(A) polymerase GLD-2/GLD-3 complex. This complex polyadenylates a set of germline C.elegans mRNAs at the entry into meiosis. I will use the structural information to understand how GLD-2/GLD-3 recognizes its substrate mRNAs and how it has diverged from the large family of canonical poly(A) polymerases. The structural analysis will allow dissecting GLD-2/GLD-3 function in vitro, and, in collaboration, to study its properties and dynamics in vivo.

• DFG-Verfahren: Sachbeihilfen
• Gastgeberin: Professorin Dr. Elena Conti