This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. RNA is an important and biological relevant molecule, which is involved in a number of critical cellular and regulatory functions. We are interested in studying the folding pathway and structural intermediate(s) of a group IIC intron from O. iheyensis ?a ~400 nt RNA. At the moment little is known about the specific features of this RNA molecule, and the structural characteristics that help it to traverse its folding landscape and correctly attain its functional native state. By observing the compaction that results from global structural transitions (Rg and Dmax) that accompany changes in the concentrations of biologically relevant and important mono- and divalent ions, and osmolytes we hope to better understand the architecture of this RNA. Moreover, SAXS data can be readily combined with information from biochemical experiments to yield nucleotide specific information on the sites of metal binding and localization within the RNA, which will illuminate what local structural transitions occur concurrently with global transformations.
The specific aims of this research is to establish a better understanding of the general processes of folding and RNA architecture as they relate to basic structural features of RNA. I have a background in utilizing NMR spectroscopy and residual dipolar coupling experiments to study the structure and dynamics of RNA junctions and motifs. I have attended a couple of short SAXS courses in the last year (2-day course by NSLS at BNL, and an 8-day course by EMBL-Hamburg at DESY), and I am currently working on new methods to study the structure and dynamics from analyses of RNA molecules through SAXS measurements and various biochemical footprinting data.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001646-29
Application #
8363552
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2011-07-01
Project End
2012-06-30
Budget Start
2011-07-01
Budget End
2012-06-30
Support Year
29
Fiscal Year
2011
Total Cost
$4,975
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
Kozlov, Guennadi; Wong, Kathy; Gehring, Kalle (2018) Crystal structure of the Legionella effector Lem22. Proteins 86:263-267
Ménade, Marie; Kozlov, Guennadi; Trempe, Jean-François et al. (2018) Structures of ubiquitin-like (Ubl) and Hsp90-like domains of sacsin provide insight into pathological mutations. J Biol Chem 293:12832-12842
Xu, Jie; Kozlov, Guennadi; McPherson, Peter S et al. (2018) A PH-like domain of the Rab12 guanine nucleotide exchange factor DENND3 binds actin and is required for autophagy. J Biol Chem 293:4566-4574
Dean, Dexter N; Rana, Pratip; Campbell, Ryan P et al. (2018) Propagation of an A? Dodecamer Strain Involves a Three-Step Mechanism and a Key Intermediate. Biophys J 114:539-549
Chen, Yu Seby; Kozlov, Guennadi; Fakih, Rayan et al. (2018) The cyclic nucleotide-binding homology domain of the integral membrane protein CNNM mediates dimerization and is required for Mg2+ efflux activity. J Biol Chem 293:19998-20007
Xu, Caishuang; Kozlov, Guennadi; Wong, Kathy et al. (2016) Crystal Structure of the Salmonella Typhimurium Effector GtgE. PLoS One 11:e0166643
Cogliati, Massimo; Zani, Alberto; Rickerts, Volker et al. (2016) Multilocus sequence typing analysis reveals that Cryptococcus neoformans var. neoformans is a recombinant population. Fungal Genet Biol 87:22-9
Oot, Rebecca A; Kane, Patricia M; Berry, Edward A et al. (2016) Crystal structure of yeast V1-ATPase in the autoinhibited state. EMBO J 35:1694-706
Lucido, Michael J; Orlando, Benjamin J; Vecchio, Alex J et al. (2016) Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry. Biochemistry 55:1226-38
Bauman, Joseph D; Harrison, Jerry Joe E K; Arnold, Eddy (2016) Rapid experimental SAD phasing and hot-spot identification with halogenated fragments. IUCrJ 3:51-60

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