Nicholas Gladman
B.A. in Biochemistry and Molecular Biology, Wittenberg University 2008
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The Arabidopsis thaliana 26S Proteasome, a large multimeric complex that degrades proteins tagged with ubiquitin, functions as the major protein degradation system in plants and other eukaryotes. I’m genetically and biochemically characterizing the interacting subunits that comprise the 19S Regulatory Particle (RP) complex of the Proteasome holeoenzyme, including the subunit RPN13. I am also using a genetic and biochemical approach to investigate the role of an alternative capping protein to the 19S RP, the PA200 particle, which could have a separate, distinct function from the 19S RP within the cell. PA200 has been implicated in DNA-damage repair due to its localization to chromatin after ionizing radiation and bleomycin treatment in yeast. However, no concrete roll for PA200 has been delineated in plants. Another project in development is the search for the major transcription factor RPN4 that has been identified in yeast, but not in plants, and is responsible for sweeping Proteasome subunit upregulation in response to Proteasome stressors like MG132.