The most abundant cation and osmolyte in the cytoplasm of E. coli, K+, has been used in studies of molecular interactions of DNA, proteins, ribosome and ions via 39K NMR. In our previous experiments, a large transverse relaxation rate of 39K has been observed in dense slurries of E. coli cells. Since the interaction of the K nucleus with the surrounding electric field gradient of the DNA dominants the 39K transverse relaxation in a K-DNA solution with little salt added, it was considered as the explanation for the 39K relaxation measured in vivo. However, the relaxation rate of 39K in DNA solutions, even with a very high concentration (i.e., physiological conditions), is much slower than that in vivo. Similar results were obtained for concentrated K-BSA and KCl solutions. The only in vitro solution that gives rise to the same large magnitude of the transverse relaxation rate as in vivo are ribosome solutions, the highly negative charged ribosome particles that have the most nucleic acids in the cell. Therefore, ribosome particles are considered as the key element that enhances the transverse relaxation of 39K in vivo. The similar characteristic of transverse relaxation was also observed in 23Na-ribosome solutions. These results require further experimental studies to confirm and to explore the molecular nature of the ribosome particle and K+, Na+-ribosome interactions. We will be using the DMX 400 spectrometer with the 10mm BB probe for both 39K and 23Na (a more sensitive nucleus) NMR studies.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002301-15
Application #
6298205
Study Section
Project Start
1999-03-01
Project End
2000-02-29
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
15
Fiscal Year
1999
Total Cost
Indirect Cost
Name
University of Wisconsin Madison
Department
Type
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
Dominguez, Eddie; Zarnowski, Robert; Sanchez, Hiram et al. (2018) Conservation and Divergence in the Candida Species Biofilm Matrix Mannan-Glucan Complex Structure, Function, and Genetic Control. MBio 9:
Franco, Aldo; Dovell, Sanaz; Möller, Carolina et al. (2018) Structural plasticity of mini-M conotoxins - expression of all mini-M subtypes by Conus regius. FEBS J 285:887-902
Wales, Jessica A; Chen, Cheng-Yu; Breci, Linda et al. (2018) Discovery of stimulator binding to a conserved pocket in the heme domain of soluble guanylyl cyclase. J Biol Chem 293:1850-1864
Travers, Timothy; López, Cesar A; Van, Que N et al. (2018) Molecular recognition of RAS/RAF complex at the membrane: Role of RAF cysteine-rich domain. Sci Rep 8:8461
Thomas, Nathan E; Wu, Chao; Morrison, Emma A et al. (2018) The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release. J Biol Chem 293:19137-19147
Assadi-Porter, Fariba M; Radek, James; Rao, Hongyu et al. (2018) Multimodal Ligand Binding Studies of Human and Mouse G-Coupled Taste Receptors to Correlate Their Species-Specific Sweetness Tasting Properties. Molecules 23:
Wijayatunga, Nadeeja N; Sams, Valerie G; Dawson, John A et al. (2018) Roux-en-Y gastric bypass surgery alters serum metabolites and fatty acids in patients with morbid obesity. Diabetes Metab Res Rev 34:e3045
Assadi-Porter, Fariba M; Reiland, Hannah; Sabatini, Martina et al. (2018) Metabolic Reprogramming by 3-Iodothyronamine (T1AM): A New Perspective to Reverse Obesity through Co-Regulation of Sirtuin 4 and 6 Expression. Int J Mol Sci 19:
Selen Alpergin, Ebru S; Bolandnazar, Zeinab; Sabatini, Martina et al. (2017) Metabolic profiling reveals reprogramming of lipid metabolic pathways in treatment of polycystic ovary syndrome with 3-iodothyronamine. Physiol Rep 5:
Mong, Surin K; Cochran, Frank V; Yu, Hongtao et al. (2017) Heterochiral Knottin Protein: Folding and Solution Structure. Biochemistry 56:5720-5725

Showing the most recent 10 out of 613 publications