This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. NO acts as a signaling molecule in a wide range of physiological processes in both eukaryotes and prokaryotes. In plants, NO participates in growth, development, flowering, and response to biotic and abiotic stresses. It has been shown that nitric oxide plays an important role in plant disease resistance. However, unlike our appreciation of NO functioning in animals, the origin and the quantification of plant NO responses to stimuli remain unclear. A comprehensive understanding of NO biology is dependent on the development of reliable NO detection methods, and EPR represents a reliable tool in this respect. Stabilization of NO radical with spin trap complexes and its detection by ESR offer the advantage of being both selective and sensitive. Initial ESR study in ACERT using NO spin trap Fe(DETC)2 showed that the model plant Arabidopsis thaliana responds to the stress caused by infiltration with Pseudomonas syringae by more rapid and robust production of NO. The Dan Klessig group is interested in using lipophilic Fe(DETC)2 complex or hydrophilic Fe(MGD)2 spin traps to evaluate NO formation in the context of plant-microbe interactions in 1) plant cell suspensions (tobacco cells) elicited for NO production with cryptogein, a 10 kDa protein secreted by the oomycete Phytophtora cryptogea that induces host defense responses, and 2) in Arabidopsis plants infected with either a bacterial pathogen (Pseudomonas syringae) or a peptide elicitor corresponding to the conserved domain of bacterial flagellin. We currently use 15N substitution to exploit the ability of the ESR measurement to distinguish between 14NO and 15NO, and we are confident that an ESR-based approach will help to elucidate the origin(s) of this radical in planta.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR016292-09
Application #
7956731
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2009-09-01
Project End
2010-08-31
Budget Start
2009-09-01
Budget End
2010-08-31
Support Year
9
Fiscal Year
2009
Total Cost
$3,864
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Jain, Rinku; Vanamee, Eva S; Dzikovski, Boris G et al. (2014) An iron-sulfur cluster in the polymerase domain of yeast DNA polymerase ?. J Mol Biol 426:301-8
Pratt, Ashley J; Shin, David S; Merz, Gregory E et al. (2014) Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes. Proc Natl Acad Sci U S A 111:E4568-76
Georgieva, Elka R; Borbat, Peter P; Ginter, Christopher et al. (2013) Conformational ensemble of the sodium-coupled aspartate transporter. Nat Struct Mol Biol 20:215-21
Airola, Michael V; Sukomon, Nattakan; Samanta, Dipanjan et al. (2013) HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. PLoS Biol 11:e1001479
Airola, Michael V; Huh, Doowon; Sukomon, Nattakan et al. (2013) Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling. J Mol Biol 425:886-901
Sun, Yan; Zhang, Ziwei; Grigoryants, Vladimir M et al. (2012) The internal dynamics of mini c TAR DNA probed by electron paramagnetic resonance of nitroxide spin-labels at the lower stem, the loop, and the bulge. Biochemistry 51:8530-41
Smith, Andrew K; Freed, Jack H (2012) Dynamics and ordering of lipid spin-labels along the coexistence curve of two membrane phases: an ESR study. Chem Phys Lipids 165:348-61
Yu, Renyuan Pony; Darmon, Jonathan M; Hoyt, Jordan M et al. (2012) High-Activity Iron Catalysts for the Hydrogenation of Hindered, Unfunctionalized Alkenes. ACS Catal 2:1760-1764
Gaffney, Betty J; Bradshaw, Miles D; Frausto, Stephen D et al. (2012) Locating a lipid at the portal to the lipoxygenase active site. Biophys J 103:2134-44
Dzikovski, Boris; Tipikin, Dmitriy; Freed, Jack (2012) Conformational distributions and hydrogen bonding in gel and frozen lipid bilayers: a high frequency spin-label ESR study. J Phys Chem B 116:6694-706

Showing the most recent 10 out of 72 publications