Group Leader

Dr. rer. nat. Andrea BARTA

My research interests center on how the structure of RNP complexes relates to their particular function. It is one of the key questions to dissect the contributions of RNA and proteins to the various activities of the RNP particle. My group is investigating two RNP complexes which carry out vital biochemical reactions: the ribosome which catalyzes peptide bond formation, and the spliceosome which catalyzes transesterification reactions. Although similar in their overall composition, these two RNP particles show interesting differences in their mechanical sequential action. The ribosome consists of two RNP subunits which assemble on a mRNA and allow the sequential decoding of genetic information and peptide bond formation until the end of the message. Most ribosomal proteins are stably bound to the three ribosomal RNAs whereas a small number of defined protein factors help to optimize the elongation cycle. In contrast, the spliceosome consists of 5 snRNP particles which assemble with many additional proteins on each intron separately. In the course of performing the two splicing steps the spliceosome has to undergo persistent changes in composition and structure. These changes require a set of proteins with specific enzymatic activities. Hence the focus of our research differs in each case: whereas in the case of the ribosome we want to investigate the contribution of the ribosomal RNA to peptide bond formation and to ribosomal dynamics, our interest in the spliceosome focuses mainly on the problem of splice site recognition and how the variability of this process influences gene expression and consequently organ development