Faculty Profile: Gershon, Paul

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Faculty Information Lab Information (Packet Type, Course Title, & Department) Location
Gershon, Paul
Lab Contact:
Paul Gershon
(949) 824-9606, 7954
Department: Virology. Molecular Biology & Biochemistry
1222 Natural Sciences 1

Research Description

I am active in four areas: (1) We operate a protein (proteomics mass spectrometry facility containing two powerful, state-of-the-art tandem mass spectrometers along with nanoflow/nanocapillary two-dimensional peptide fractionation HPLC with robotics. Last year, several 199s deftly learned to operate these instruments and used them to, among other things, identify all the proteins in some of the world_ largest viruses. We will now be identifying and quantitating the proteins characteristic of diseased/tumorigenic cells and developmental abnormalities. (2) My lab is currently funded to investigate the structure and molecular dynamics of the enzyme poly(A) polymerase (PAP), using the vaccinia virus enzyme as a model. The vaccinia PAP was the first PAP for which a gene was identified (by the P.I.), and we recently learned its three-dimensional structure. Vaccinia PAP is the only known polymerase that can translocate independently on single-stranded nucleic acid. How does it do this on a non-rigid polymer? Come to my lab and solve the mystery. (3) A collaboration between my lab and that of Dr. Alex McPherson (MB&B) has led to the clearest images obtained thus far of vaccinia virus particles and subviral assemblies, providing a unique opportunity to identify viral proteins and functions present in various subviral assemblies. This dovetails well with protein mass spectrometry (above). (4) I am also funded to investigate the catalytic mechanism of RNA O-methylation. Vaccinia virus protein VP39 provided the first three-dimensional structure for any poxvirus protein and any RNA methyltransferase. The structure was then solved again, with bound RNA substrate and cofactor. Using various chemical, biochemical and NMR techniques, we are elucidating aspects of its catalytic mechanism from hypotheses arising from the three-dimensional structure. Overall, prior undergraduate interns in my lab have been included as authors on manuscripts submitted for publication, and some current ones will be.