@article{thomas_herrero_eng_gomaa_gillikin_noar_beseli_daub_2020, title={Engineering Cercospora disease resistance via expression of Cercospora nicotianae cercosporin-resistance genes and silencing of cercosporin production in tobacco}, volume={15}, ISSN={1932-6203}, url={http://dx.doi.org/10.1371/journal.pone.0230362}, DOI={10.1371/journal.pone.0230362}, abstractNote={Fungi in the genus Cercospora cause crop losses world-wide on many crop species. The wide host range and success of these pathogens has been attributed to the production of a photoactivated toxin, cercosporin. We engineered tobacco for resistance to Cercospora nicotianae utilizing two strategies: 1) transformation with cercosporin autoresistance genes isolated from the fungus, and 2) transformation with constructs to silence the production of cercosporin during disease development. Three C. nicotianae cercosporin autoresistance genes were tested: ATR1 and CFP, encoding an ABC and an MFS transporter, respectively, and 71cR, which encodes a hypothetical protein. Resistance to the pathogen was identified in transgenic lines expressing ATR1 and 71cR, but not in lines transformed with CFP. Silencing of the CTB1 polyketide synthase and to a lesser extent the CTB8 pathway regulator in the cercosporin biosynthetic pathway also led to the recovery of resistant lines. All lines tested expressed the transgenes, and a direct correlation between the level of transgene expression and disease resistance was not identified in any line. Resistance was also not correlated with the degree of silencing in the CTB1 and CTB8 silenced lines. We conclude that expression of fungal cercosporin autoresistance genes as well as silencing of the cercosporin pathway are both effective strategies for engineering resistance to Cercospora diseases where cercosporin plays a critical role.}, number={3}, journal={PLOS ONE}, publisher={Public Library of Science (PLoS)}, author={Thomas, Elizabeth and Herrero, Sonia and Eng, Hayde and Gomaa, Nafisa and Gillikin, Jeff and Noar, Roslyn and Beseli, Aydin and Daub, Margaret E.}, editor={Wilson, Richard A.Editor}, year={2020}, month={Mar}, pages={e0230362} }
 @article{selote_matthiadis_gillikin_sato_long_2018, title={The E3 ligase BRUTUS facilitates degradation of VOZ1/2 transcription factors}, volume={41}, ISSN={["1365-3040"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-85050368197&partnerID=MN8TOARS}, DOI={10.1111/pce.13363}, abstractNote={Abstract}, number={10}, journal={PLANT CELL AND ENVIRONMENT}, publisher={Wiley}, author={Selote, Devarshi and Matthiadis, Anna and Gillikin, Jeffrey W. and Sato, Masa H. and Long, Terri A.}, year={2018}, month={Oct}, pages={2463–2474} }
 @article{selote_samira_matthiadis_gillikin_long_2015, title={Iron-Binding E3 Ligase Mediates Iron Response in Plants by Targeting Basic Helix-Loop-Helix Transcription Factors}, volume={167}, ISSN={["1532-2548"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84920141665&partnerID=MN8TOARS}, DOI={10.1104/pp.114.250837}, abstractNote={Abstract}, number={1}, journal={PLANT PHYSIOLOGY}, author={Selote, Devarshi and Samira, Rozalynne and Matthiadis, Anna and Gillikin, Jeffrey W. and Long, Terri A.}, year={2015}, month={Jan}, pages={273-+} }
 @article{rueschhoff_gillikin_sederoff_daub_2013, title={The SOS4 pyridoxal kinase is required for maintenance of vitamin B-6-mediated processes in chloroplasts}, volume={63}, ISSN={["0981-9428"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84872415352&partnerID=MN8TOARS}, DOI={10.1016/j.plaphy.2012.12.003}, abstractNote={Vitamin B(6) (pyridoxal 5'-phosphate and its vitamers) is an important cofactor in numerous enzymatic reactions. In spite of its importance, the consequences of altering vitamin B(6) content on plant growth and development are not well understood. This study compares two mutants for vitamin B(6)-metabolizing enzymes in Arabidopsis thaliana: a pdx1.3 mutant in the de novo synthesis pathway and a salvage pathway sos4 mutant that accumulates more vitamin B(6). We show that despite a difference in total B(6) content in leaf tissue, both mutants share similar phenotypes, including chlorosis, decreased size, altered chloroplast ultrastructure, and root sensitivity to sucrose. Assay of B(6) vitamer content from isolated chloroplasts showed that, despite differing B(6) vitamer content in whole leaf tissue, both mutants share a common deficiency in total and phosphorylated vitamers in chloroplasts. One of the splice variants of the SOS4 proteins was shown to be located in the chloroplast. Our data indicate that some of the phenotypic consequences shared between the pdx1.3 and sos4 mutants are due to B(6) deficiency in chloroplasts, and show that SOS4 is required for maintenance of phosphorylated B(6) vitamer concentrations in chloroplasts. Further, our data are consistent with a diffusion model for transport of vitamin B(6) into chloroplasts.}, journal={PLANT PHYSIOLOGY AND BIOCHEMISTRY}, author={Rueschhoff, Elizabeth E. and Gillikin, Jeffrey W. and Sederoff, Heike W. and Daub, Margaret E.}, year={2013}, month={Feb}, pages={281–291} }
 @article{herrero_gonzalez_gillikin_velez_daub_2011, title={Identification and characterization of a pyridoxal reductase involved in the vitamin B6 salvage pathway in Arabidopsis}, volume={76}, ISSN={["1573-5028"]}, DOI={10.1007/s11103-011-9777-x}, abstractNote={Vitamin B6 (pyridoxal phosphate) is an essential cofactor in enzymatic reactions involved in numerous cellular processes and also plays a role in oxidative stress responses. In plants, the pathway for de novo synthesis of pyridoxal phosphate has been well characterized, however only two enzymes, pyridoxal (pyridoxine, pyridoxamine) kinase (SOS4) and pyridoxamine (pyridoxine) 5' phosphate oxidase (PDX3), have been identified in the salvage pathway that interconverts between the six vitamin B6 vitamers. A putative pyridoxal reductase (PLR1) was identified in Arabidopsis based on sequence homology with the protein in yeast. Cloning and expression of the AtPLR1 coding region in a yeast mutant deficient for pyridoxal reductase confirmed that the enzyme catalyzes the NADPH-mediated reduction of pyridoxal to pyridoxine. Two Arabidopsis T-DNA insertion mutant lines with insertions in the promoter sequences of AtPLR1 were established and characterized. Quantitative RT-PCR analysis of the plr1 mutants showed little change in expression of the vitamin B6 de novo pathway genes, but significant increases in expression of the known salvage pathway genes, PDX3 and SOS4. In addition, AtPLR1 was also upregulated in pdx3 and sos4 mutants. Analysis of vitamer levels by HPLC showed that both plr1 mutants had lower levels of total vitamin B6, with significantly decreased levels of pyridoxal, pyridoxal 5'-phosphate, pyridoxamine, and pyridoxamine 5'-phosphate. By contrast, there was no consistent significant change in pyridoxine and pyridoxine 5'-phosphate levels. The plr1 mutants had normal root growth, but were significantly smaller than wild type plants. When assayed for abiotic stress resistance, plr1 mutants did not differ from wild type in their response to chilling and high light, but showed greater inhibition when grown on NaCl or mannitol, suggesting a role in osmotic stress resistance. This is the first report of a pyridoxal reductase in the vitamin B6 salvage pathway in plants.}, number={1-2}, journal={PLANT MOLECULAR BIOLOGY}, author={Herrero, Sonia and Gonzalez, Eugenia and Gillikin, Jeffrey W. and Velez, Heriberto and Daub, Margaret E.}, year={2011}, month={May}, pages={157–169} }
 @article{kim_gibbon_gillikin_larkins_boston_jung_2006, title={The maize Mucronate mutation is a deletion in the 16-kDa gamma-zein gene that induces the unfolded protein response}, volume={48}, ISSN={["0960-7412"]}, DOI={10.1111/j.1365-313X.2006.02884.x}, abstractNote={Summary}, number={3}, journal={PLANT JOURNAL}, author={Kim, Cheol Soo and Gibbon, Bryan C. and Gillikin, Jeffrey W. and Larkins, Brian A. and Boston, Rebecca S. and Jung, Rudolf}, year={2006}, month={Nov}, pages={440–451} }
 @article{pagny_cabanes-macheteau_gillikin_leborgne-castel_lerouge_boston_faye_gomord_2000, title={Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention}, volume={12}, ISSN={["1531-298X"]}, DOI={10.1105/tpc.12.5.739}, abstractNote={Using pulse–chase experiments combined with immunoprecipitation and N-glycan structural analysis, we showed that the retrieval mechanism of proteins from post–endoplasmic reticulum (post-ER) compartments is active in plant cells at levels similar to those described previously for animal cells. For instance, recycling from the Golgi apparatus back to the ER is sufficient to block the secretion of as much as 90% of an extracellular protein such as the cell wall invertase fused with an HDEL C-terminal tetrapeptide. Likewise, recycling can sustain fast retrograde transport of Golgi enzymes into the ER in the presence of brefeldin A. However, on the basis of our data, we propose that this retrieval mechanism in plants has little impact on the ER retention of a soluble ER protein such as calreticulin. Indeed, the latter is retained in the ER without any N-glycan–related evidence for a recycling through the Golgi apparatus. Taken together, these results indicate that calreticulin and perhaps other plant reticuloplasmins are possibly largely excluded from vesicles exported from the ER. Instead, they are probably retained in the ER by mechanisms that rely primarily on signals other than H/KDEL motifs.}, number={5}, journal={PLANT CELL}, author={Pagny, S and Cabanes-Macheteau, M and Gillikin, JW and Leborgne-Castel, N and Lerouge, P and Boston, RS and Faye, L and Gomord, V}, year={2000}, month={May}, pages={739–755} }
 @article{gillikin_zhang_coleman_bass_larkins_boston_1997, title={A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane}, volume={114}, ISSN={["0032-0889"]}, DOI={10.1104/pp.114.1.345}, abstractNote={Abstract}, number={1}, journal={PLANT PHYSIOLOGY}, author={Gillikin, JW and Zhang, F and Coleman, CE and Bass, HW and Larkins, BA and Boston, RS}, year={1997}, month={May}, pages={345–352} }
 @article{boston_gillikin_wrobel_zhang_1997, title={Molecular chaperone activity of er-resident proteins in seeds}, volume={16}, number={1997}, journal={Current Topics in Plant Biochemistry and Physiology}, author={Boston, R. S. and Gillikin, J. W. and Wrobel, R. L. and Zhang, F.}, year={1997}, pages={3–4} }