Education & Certifications


  • Bachelor of Science, UC Berkeley, Microbial Biology (2012)

Current Research and Scholarly Interests


The genetic and physical basis of silica nano-patterning in diatom algae.

All Publications


  • Diel transcriptomics in the model diatom Thalassiosira pseudonana reveal key metabolic strategies J Phycology (In Process) Russell, J. J., Theriot, J. A. 2018
  • Genetic and biochemical approaches toward understanding diatom cell shape and nanopatterning Diatom Morphogenesis Russell, J. J., Theriot, J. A. Wiley-Scrivener. 2018
  • Development of a robust live cell fluorescence microscopy platform for diatoms In Process Russell, J. J., Renner, L. D., Theriot, J. A. 2018
  • GreenCut protein CPLD49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b6f complex accumulation. The Plant journal : for cell and molecular biology Wittkopp, T. M., Saroussi, S., Yang, W., Johnson, X., Kim, R. G., Heinnickel, M. L., Russell, J. J., Phuthong, W., Dent, R. M., Broeckling, C. D., Peers, G., Lohr, M., Wollman, F. A., Niyogi, K. K., Grossman, A. R. 2018

    Abstract

    The GreenCut encompasses a suite of nucleus-encoded proteins with orthologs among green lineage organisms (plants, green algae), but that are absent or poorly conserved in non-photosynthetic/heterotrophic organisms. In Chlamydomonas reinhardtii, CPLD49 (Conserved in Plant Lineage and Diatoms49) is an uncharacterized GreenCut protein that is critical for maintaining normal photosynthetic function. We demonstrate that a cpld49 mutant has impaired photoautotrophic growth under high light conditions. The mutant exhibits a nearly 90% reduction in the level of the cytochrome b6f complex (Cytb6f), which impacts linear and cyclic electron transport, but does not compromise the ability of the strain to perform state transitions. Furthermore, CPLD49 strongly associates with thylakoid membranes where it may be part of a membrane protein complex with another GreenCut protein, CPLD38; a mutant null for CPLD38 also impacts Cytb6f complex accumulation. We investigated several potential functions of CPLD49, with some suggested by protein homology. Our findings are congruent with the hypothesis that CPLD38 and CPLD49 are part of a novel thylakoid membrane complex that primarily modulates accumulation, but also impacts the activity of the Cytb6f complex. Based on motifs of CPLD49 and the activities of other CPLD49-like proteins, we suggest a role for this putative dehydrogenase in the synthesis of a lipophilic thylakoid membrane molecule that influences the assembly and activity of Cytb6f. This article is protected by copyright. All rights reserved.

    View details for DOI 10.1111/tpj.13915

    View details for PubMedID 29602195

  • Comparative transcriptomics of Phaeodactylum tricornutum morphotypes reveal key genes associated with cell shape In Process Russell, J. J., Theriot, J. A. 2018
  • Non-model model organisms. BMC biology Russell, J. J., Theriot, J. A., Sood, P., Marshall, W. F., Landweber, L. F., Fritz-Laylin, L., Polka, J. K., Oliferenko, S., Gerbich, T., Gladfelter, A., Umen, J., Bezanilla, M., Lancaster, M. A., He, S., Gibson, M. C., Goldstein, B., Tanaka, E. M., Hu, C. K., Brunet, A. 2017; 15 (1): 55

    Abstract

    Model organisms are widely used in research as accessible and convenient systems to study a particular area or question in biology. Traditionally only a handful of organisms have been widely studied, but modern research tools are enabling researchers to extend the set of model organisms to include less-studied and more unusual systems. This Forum highlights a range of 'non-model model organisms' as emerging systems for tackling questions across the whole spectrum of biology (and beyond), the opportunities and challenges, and the outlook for the future.

    View details for DOI 10.1186/s12915-017-0391-5

    View details for PubMedID 28662661

    View details for PubMedCentralID PMC5492503

  • A Conserved Rubredoxin Is Necessary for Photosystem II Accumulation in Diverse Oxygenic Photoautotrophs JOURNAL OF BIOLOGICAL CHEMISTRY Calderon, R. H., Garcia-Cerdan, J. G., Malnoe, A., Cook, R., Russell, J. J., Gaw, C., Dent, R. M., de Vitry, C., Niyogi, K. K. 2013; 288 (37): 26688-26696

    Abstract

    In oxygenic photosynthesis, two photosystems work in tandem to harvest light energy and generate NADPH and ATP. Photosystem II (PSII), the protein-pigment complex that uses light energy to catalyze the splitting of water, is assembled from its component parts in a tightly regulated process that requires a number of assembly factors. The 2pac mutant of the unicellular green alga Chlamydomonas reinhardtii was isolated and found to have no detectable PSII activity, whereas other components of the photosynthetic electron transport chain, including photosystem I, were still functional. PSII activity was fully restored by complementation with the RBD1 gene, which encodes a small iron-sulfur protein known as a rubredoxin. Phylogenetic evidence supports the hypothesis that this rubredoxin and its orthologs are unique to oxygenic phototrophs and distinct from rubredoxins in Archaea and bacteria (excluding cyanobacteria). Knockouts of the rubredoxin orthologs in the cyanobacterium Synechocystis sp. PCC 6803 and the plant Arabidopsis thaliana were also found to be specifically affected in PSII accumulation. Taken together, our data suggest that this rubredoxin is necessary for normal PSII activity in a diverse set of organisms that perform oxygenic photosynthesis.

    View details for DOI 10.1074/jbc.M113.487629

    View details for Web of Science ID 000330594500034

    View details for PubMedID 23900844

    View details for PubMedCentralID PMC3772215