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Protein Science (2004), 13:342-350. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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High-temperature solution NMR structure of TmCsp

Astrid Jung, Christian Bamann, Werner Kremer, Hans Robert Kalbitzer and Eike Brunner

University of Regensburg, Institute of Biophysics and Physical Biochemistry, D-93040 Regensburg, Germany

(RECEIVED June 30, 2003; FINAL REVISION September 29, 2003; ACCEPTED October 2, 2003)



Abstract

Cold shock proteins (Csps) are assumed to play a central role in the regulation of gene expression under cold shock conditions. Acting as single-stranded nucleic acid-binding proteins, they trigger the translation process and are therefore involved in the compensation of the influence of low temperatures (cold shock) upon the cell metabolism. However, it is unknown so far how Csps are switched on and off as a function of temperature. The aim of the present study is the study of possible structural changes responsible for this switching process. 1H-15N HSQC spectra recorded at different temperatures and chemical-shift analysis have indicated subtle conformational changes for the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima (TmCsp) when the temperature is elevated from 303 K to its physiological temperature (343 K). The three-dimensional structure of TmCsp was determined by nuclear magnetic resonance (NMR) spectroscopy at 343 K to obtain quantitative information concerning these structural changes. By use of residual dipolar couplings, the loss of NOE information at high temperature could be compensated successfully. Most pronounced conformational changes compared with room-temperature conditions are observed for amino acid residues closely neighbored to two characteristic {beta}-bulges and a well-defined loop region of the protein. Because the residues shown to be responsible for the interaction of TmCsp with single-stranded nucleic acids can almost exclusively be found within these regions, nucleic acid-binding activity might be down-regulated with increasing temperature by the described conformational changes.

Keywords: Cold shock protein; NMR; residual dipolar couplings; thermophilic adaptation; RNA binding

Abbreviations: COSY, correlation spectroscopy • NOE, nuclear Overhauser effect • NOESY, nuclear Overhauser effect spectroscopy • TOCSY, total correlation spectroscopy • HSQC, heteronuclear single quantum coherence • DSS, Sodium-2,2-dimethyl-2-silapentane-5-sulfonate • MOCCA, modified phase-cycled Carr-Purcell • SIAM, simultaneous acquisition of in-phase and anti-phase multiplets • rmsd, root mean square deviation • ssDNA, single-stranded DNA • Csp, cold shock protein • Tm, Thermotoga maritima • TmCsp, cold shock protein from Thermotoga maritima • Tm, melting temperature • ppb, parts per billion • ppm, parts per million • {Phi}, {Psi}, backbone torsion angles • DMPC, DiMyristoyl Phosphatidyl Choline • DHPC, DiHexanoyl Phosphatidyl Choline • CTAB, hexadecyl (Cetyl) Trimethyl Ammonium Bromide • CNS, crystallography and NMR system • RNP, RiboNucleoProtein

Reprint requests to: Eike Brunner, University of Regensburg, Institute of Biophysics and Physical Biochemistry, D-93040 Regensburg, Germany; e-mail: eike.brunner{at}biologie.uni-regensburg.de; fax: 49-941-943-2479.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03281604.


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[Abstract] [Full Text] [PDF]


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