The nuclear magnetic resonance (NMR) spectrometer subject of this application supports a wide range of research among numerous investigators at UT Southwestern Medical Center. It allows the study of protein structure, dynamics, and molecular interactions on medically and biologically relevant systems. For example, Dr. Michael Rosen studies cytoskeletal dynamics, an important biological process involved in cell migration, adhesion, establishment and maintenance of polarity, and vesicle trafficking. Dr. Jose Rizo-Rey aims to understand the regulation of neurotransmitter release by proteins involved in membrane fusion. Dr. Kevin Gardner is interested in how signal transduction of environmental cues, like xenobiotics, light, and oxygen are ultimately involved in gene regulation. Dr. Xuelian Luo is characterizing the regulation of the spindle checkpoint signaling during cell mitosis, the chromosome inheritance point of the cell cycle. These systems are important to basic biology and to developing new methods to diagnose and treat human disease. The NMR spectrometer is over 10 years old, and uses technology no longer produced by the instrument manufacturer. Repairs are increasingly frequent and expensive, take longer, and soon will not be possible. This proposal requests funds to purchase a new 600MHz NMR spectrometer console. The console is the heart of a NMR spectrometer since it contains all the digital and radiofrequency electronics necessary to acquire NMR experiments. This equipment will continue supporting NIH-funded programs in the laboratories of Dr. Michael Rosen, Dr. Jose Rizo-Rey, Dr. Kevin Gardner, and Dr. Xuelian Luo, thus facilitating the above stated research. Additionally, this equipment will also be available to the UT Southwestern community in need of NMR data for biophysical studies on an even wider range of important biological processes.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR026461-01
Application #
7792178
Study Section
Special Emphasis Panel (ZRG1-BCMB-N (30))
Program Officer
Levy, Abraham
Project Start
2010-07-20
Project End
2012-07-19
Budget Start
2010-07-20
Budget End
2012-07-19
Support Year
1
Fiscal Year
2010
Total Cost
$254,200
Indirect Cost
Name
University of Texas Sw Medical Center Dallas
Department
Biochemistry
Type
Schools of Medicine
DUNS #
800771545
City
Dallas
State
TX
Country
United States
Zip Code
75390
de Jong, Arthur P H; Roggero, Carlos M; Ho, Meng-Ru et al. (2018) RIM C2B Domains Target Presynaptic Active Zone Functions to PIP2-Containing Membranes. Neuron 98:335-349.e7
Jensen, Jaime L; Wu, Qiong; Colbert, Christopher L (2018) NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB. Biomol NMR Assign 12:91-94
Yoshizawa, Takuya; Ali, Rustam; Jiou, Jenny et al. (2018) Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. Cell 173:693-705.e22
Voleti, Rashmi; Tomchick, Diana R; Südhof, Thomas C et al. (2017) Exceptionally tight membrane-binding may explain the key role of the synaptotagmin-7 C2A domain in asynchronous neurotransmitter release. Proc Natl Acad Sci U S A 114:E8518-E8527
Pan, Yun-Zu; Quade, Bradley; Brewer, Kyle D et al. (2016) Sequence-specific assignment of methyl groups from the neuronal SNARE complex using lanthanide-induced pseudocontact shifts. J Biomol NMR 66:281-293
Ouyang, Zhuqing; Zheng, Ge; Tomchick, Diana R et al. (2016) Structural Basis and IP6 Requirement for Pds5-Dependent Cohesin Dynamics. Mol Cell 62:248-259
Clark, Lindsay; Zahm, Jacob A; Ali, Rustam et al. (2016) Erratum to: Methyl labeling and TROSY NMR spectroscopy of proteins expressed in the eukaryote Pichia pastoris. J Biomol NMR 64:267
Banjade, Sudeep; Wu, Qiong; Mittal, Anuradha et al. (2015) Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck. Proc Natl Acad Sci U S A 112:E6426-35
Hara, Mayuko; Özkan, Engin; Sun, Hongbin et al. (2015) Structure of an intermediate conformer of the spindle checkpoint protein Mad2. Proc Natl Acad Sci U S A 112:11252-7
Ni, Lisheng; Zheng, Yonggang; Hara, Mayuko et al. (2015) Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling. Genes Dev 29:1416-31

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