Chartron, Justin - University of California, Riverside

个人简介

Dr. Chartron’s research group is interested in how a biological cell acts as a system to assemble proteins, and they apply this knowledge to improve yields of engineered proteins. The group develops high-throughput strategies to survey protein production from many industrially significant organisms. Machine learning and other computational tools are used to discover the genetic features associated with high levels of protein production. Dr. Chartron is also interested in designing control systems to rapidly remodel production and degradation pathways within a cell. By better understanding how cells function, his group can develop rational strategies to improve the manufacturing of commercially important proteins like enzymes, materials, and therapeutics. Prior to joining UC Riverside, Dr. Chartron was a postdoctoral fellow at Stanford University. He developed systems-level experiments that gave insight into how molecular chaperones and protein targeting factors interact with every gene product in a cell. Dr. Chartron’s graduate work at Caltech focused on the molecular mechanisms of protein targeting factors.

研究领域

Quantitative Systems BiologyBiophysics of Protein MaturationMolecular and Cellular EngineeringBiotechnologyBiopharmaceutical Production

近期论文

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Chartron, J.W., Hunt, K.C.L., and Frydman, J. (2016) Cotranslational signal-independent SRP preloading during membrane targeting. Nature 536, 224–228. Dhungel, N., Eleuteri, S., Li, L.B., Kramer, N.J., Chartron, J.W., et al. (2015) Parkinson’s disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron 85, 76–87. Mock, J.Y., Chartron, J.W., Zaslaver, M., Xu, Y., Ye, Y., and Clemons, W.M. (2015) Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain. Proc. Natl. Acad. Sci. U.S.A. 112, 106–111. Gristick, H.B, Rome, M.E., Chartron, J.W., Rao, M., Hess, S., Shan, S.O., and Clemons, W.M. (2015) Mechanism of assembly of a substrate transfer complex during tail-anchored protein targeting. J. Biol. Chem. 290, 30006–30017. Pechmann, S., Chartron, J.W., and Frydman, J. (2014) Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo. Nat. Struct. Mol. Biol. 21, 1100–1105. Gristick, H.B., Rao, M., Chartron, J.W., Rome, M.E., Shan, S., and Clemons, W.M. (2014) Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4. Nat. Struct. Mol. Biol. 21, 437–442. Chartron, J.W., Clemons, W.M., and Suloway, C.J.M. (2012) The complex process of GETting tail-anchored membrane proteins to the ER. Curr. Opin. Struct. Biol. 22, 217–224. Chartron, J.W., VanderVelde, D.G., and Clemons, W.M. (2012) Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal a novel interaction that forms a conserved dynamic interface. Cell Rep. 2, 1620–1632. Chartron, J.W., VanderVelde, D.G., Rao, M., and Clemons, W.M. (2012) Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex. J. Biol. Chem. 287, 8310–8317. Chartron, J.W., Gonzalez, G.M., and Clemons, W.M. (2011) A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex. J. Biol. Chem. 286, 34325–34334. Chartron, J.W., Suloway, C.J.M., Zaslaver, M., and Clemons, W.M. (2010) Structural characterization of the Get4/Get5 complex and its interaction with Get3. Proc. Natl. Acad. Sci. U.S.A. 107, 12127–12132. Suloway, C.J.M., Chartron, J.W., Zaslaver, M., and Clemons, W.M. (2009) Model for eukaryotic tail- anchored protein binding based on the structure of Get3. Proc. Natl. Acad. Sci. U.S.A. 106, 14849–14854. Chandrasekar, S., Chartron, J., Jaru-Ampornpan, P., and Shan, S. (2008) Structure of the chloroplast signal recognition particle (SRP) receptor: Domain arrangement modulates SRP—receptor interaction. J. Mol. Biol. 375, 425–436. Chartron, J., Shiau, C., Stout, C.D., and Carroll, K.S. (2007) 3’-phosphoadenosine-5’-phosphosulfate reductase in complex with thioredoxin: A structural snapshot in the catalytic cycle. Biochemistry **46*8, 3942–3951. Chartron, J., Carroll, K.S., Shiau, C., Gao, H., Leary, J.A., Bertozzi, C.R., and Stout, C.D. (2006) Substrate recognition, protein dynamics and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5’-phosphosulfate reductase. J. Mol. Biol. 364, 152–169. Sundaresan, V., Chartron, J., Yamaguchi, M., and Stout, C.D. (2005) Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains. J. Mol. Biol. 346, 617–629. Sundaresan, V., Yamaguchi, M., Chartron, J., and Stout, C.D. (2003) Conformational change in the NADP(H) binding domain of transhydrogenase defines four states. Biochemistry 42, 12143–12153.