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Seminars
Building Molecular Lenses to Understand RNA-Protein Regulation In Vivo
Thursday, September 22, 2011
3:30 pm - 5:00 pm
3:30 pm - 5:00 pm
Location: BME 3.204
Presenter Information.
Abstract
Due to the importance of RNA-protein interactions in biological processes, there is considerable interest in elucidating the specific molecular features that proteins use to recognize and discriminate between the many different classes of RNAs. Although in vitro studies have contributed significantly to our knowledge of the types of sequence and structural motifs that are involved in the complexing of RNAs and proteins, complete understanding of how these macromolecular interactions form intracellularly is unclear. Moreover, little is known about how the formation of RNA-protein complexes in vivo relates to their regulatory and/or catalytic activities. We have characterized a model ribonucleoprotein particle and shown interesting correlations between its molecular traits and its functional capabilities. We have also shown the utility of manipulating ribonucleoprotein surfaces in vivo for applications in molecular engineering. Currently, we are developing high-throughput probes to quantitate RNA-protein interactions directly within cells. We have made significant progress establishing this system in Escherichia coli within the context of a stable group II intron ribonucleoprotein particle (RNP) and of transient small RNA-protein regulatory interactions. We are also building computational models to help us understand the biological relevance of observed changes in these molecular interactions. Our initial results support the interdependence between global cellular metabolism and the nature of intermolecular interactions. Increased knowledge in this area is vital to the development of new technologies and bioengineering strategies.
Abstract
Due to the importance of RNA-protein interactions in biological processes, there is considerable interest in elucidating the specific molecular features that proteins use to recognize and discriminate between the many different classes of RNAs. Although in vitro studies have contributed significantly to our knowledge of the types of sequence and structural motifs that are involved in the complexing of RNAs and proteins, complete understanding of how these macromolecular interactions form intracellularly is unclear. Moreover, little is known about how the formation of RNA-protein complexes in vivo relates to their regulatory and/or catalytic activities. We have characterized a model ribonucleoprotein particle and shown interesting correlations between its molecular traits and its functional capabilities. We have also shown the utility of manipulating ribonucleoprotein surfaces in vivo for applications in molecular engineering. Currently, we are developing high-throughput probes to quantitate RNA-protein interactions directly within cells. We have made significant progress establishing this system in Escherichia coli within the context of a stable group II intron ribonucleoprotein particle (RNP) and of transient small RNA-protein regulatory interactions. We are also building computational models to help us understand the biological relevance of observed changes in these molecular interactions. Our initial results support the interdependence between global cellular metabolism and the nature of intermolecular interactions. Increased knowledge in this area is vital to the development of new technologies and bioengineering strategies.
