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. Current year GUP-21939: This GUP is a follow-up to GUP11627(2008) and GUP12457 (2009) in which we examined the proposed general features of riboswitch conformational change upon binding cognate small-molecules. Riboswitches are gene-regulatory mRNA domains that respond to the intracellular concentration of their cognate small molecules by modulating transcription or translation in bacteria and pre-mRNA splicing or polyadenylation in eukaryotes. For all riboswitch classes examined, phylogenetic sequence analyses delineate a segment of highly conserved sequence that is necessary and sufficient for specific in vitro binding to their cognate metabolites. These specific binding domains, or aptamers, have been the central focus of studies investigating riboswitch mechanism and function. Conformational changes are thought to be an integral part of riboswitch function. Small angle X-ray scattering is a technique to probe the global nature of such conformational changes. Recently, several labs have published papers utilizing this technique to understand the metabolite-induced structural response of several riboswitch RNA. The current proposal is related to GUP12457 and GUP11627, both entitled """"""""Investigating the proposed 'switching'mechanism of various riboswitches"""""""". The previous GUPs, for which beamtime was allocated, focused on examining the proposed general features of riboswitch function. SAXS analyses revealed idiosyncratic responses of various riboswitches to their respective small-molecule effectors as described in our recent publications (Baird and Ferre-D'Amare, RNA, 2010;Kulshina et al, NSMB, 2009).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR008630-16
Application #
8361281
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2011-01-01
Project End
2011-12-31
Budget Start
2011-01-01
Budget End
2011-12-31
Support Year
16
Fiscal Year
2011
Total Cost
$9,852
Indirect Cost
Name
Illinois Institute of Technology
Department
Other Basic Sciences
Type
Schools of Arts and Sciences
DUNS #
042084434
City
Chicago
State
IL
Country
United States
Zip Code
60616
Orgel, Joseph P R O; Sella, Ido; Madhurapantula, Rama S et al. (2017) Molecular and ultrastructural studies of a fibrillar collagen from octocoral (Cnidaria). J Exp Biol 220:3327-3335
Yazdi, Aliakbar Khalili; Vezina, Grant C; Shilton, Brian H (2017) An alternate mode of oligomerization for E. coli SecA. Sci Rep 7:11747
Sullivan, Brendan; Robison, Gregory; Pushkar, Yulia et al. (2017) Copper accumulation in rodent brain astrocytes: A species difference. J Trace Elem Med Biol 39:6-13
Morris, Martha Clare (2016) Nutrition and risk of dementia: overview and methodological issues. Ann N Y Acad Sci 1367:31-7
Robison, Gregory; Sullivan, Brendan; Cannon, Jason R et al. (2015) Identification of dopaminergic neurons of the substantia nigra pars compacta as a target of manganese accumulation. Metallomics 7:748-55
Gelfand, Paul; Smith, Randy J; Stavitski, Eli et al. (2015) Characterization of Protein Structural Changes in Living Cells Using Time-Lapsed FTIR Imaging. Anal Chem 87:6025-31
Liang, Wenguang G; Ren, Min; Zhao, Fan et al. (2015) Structures of human CCL18, CCL3, and CCL4 reveal molecular determinants for quaternary structures and sensitivity to insulin-degrading enzyme. J Mol Biol 427:1345-1358
Zhou, Hao; Li, Shangyang; Badger, John et al. (2015) Modulation of HIV protease flexibility by the T80N mutation. Proteins 83:1929-39
Baird, Nathan J; Ferré-D'Amaré, Adrian R (2014) Analysis of riboswitch structure and ligand binding using small-angle X-ray scattering (SAXS). Methods Mol Biol 1103:211-25
Nobrega, R Paul; Arora, Karunesh; Kathuria, Sagar V et al. (2014) Modulation of frustration in folding by sequence permutation. Proc Natl Acad Sci U S A 111:10562-7

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