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Gideon Dreyfuss, Ph.D.

Isaac Norris Professor of Biochemistry and Biophysics
Howard Hughes Medical Institute Investigator

328 Clinical Research Building
415 Curie Blvd.
Philadelphia, PA 19104-6148
T: (215) 898-0398, 898-0172
F: (215) 573-2000
gdreyfuss@hhmi.upenn.edu

Ph.D. Harvard University (1978) Biological Chemistry

pubmed

DESCRIPTION OF RESEARCH INTERESTS:

The research efforts of the Dreyfuss laboratory are presently focused on three interrelated topics:

The structure and function of the major pre-mRNA-binding proteins (hnRNPs) and mRNA-binding proteins (mRNPs), with particular focus on the role of these proteins in the formation and function of mRNA. The significance of these proteins is that they influence the structure and interactions of pre-mRNAs and, therefore, their fate and processing into mRNAs. They also appear to function in mRNA nuclear export. Many of these proteins have been identified and studied in this laboratory, and this effort continues.

The transport of proteins and RNAs between the nucleus and the cytoplasm. The Dreyfuss lab found that while some hnRNP proteins are confined to the nucleus, many others shuttle continuously between the nucleus and the cytoplasm. The shuttling hnRNP proteins likely have a role in the export of mRNA from the nucleus to the cytoplasm. The sequences in the proteins that mediate their localization and transport, the cellular machineries involved, and their role in mRNA nuclear export have been characterized and specific nuclear export and import factors are being studied.

The molecular function of SMN (Survival of Motor Neurons), the protein product of the Spinal Muscular Atrophy disease gene, and the function of Gems: a novel nuclear structure containing the SMN protein. The Dreyfuss lab found a major nuclear structure that contains the SMN protein (the disease gene of Spinal Muscular Atrophy). It appears to have an important role in RNA polymerase II gene expression pathway. The lab recently found the molecular function of the SMN protein. It, together with a protein they call SIP1, is an essential spliceosomal snRNP assembly factor.

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