Acceleration of the refolding of Arc repressor by nucleic acids and other polyanions

作者: Robert T. Sauer , Dionisios Rentzeperis , Thorlakur Jonsson

DOI: 10.1038/9353

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摘要: The refolding rate of the Arc repressor dimer can be accelerated 30-fold or more by negatively charged polymers including single-stranded and double-stranded DNA, RNA, polyvinylsulfate but not neutral positively polymers. salt-dependence polyanion-mediated process mutant studies indicate that electrostatic interactions are important in acceleration. Urea-dependence suggest is relatively unstructured transition state for polyanion-stimulated refolding. At low ionic strength, observed kinetics consistent with a model which denatured monomers bind rapidly nonspecifically to polyanion complete folding bound state.

参考文章(21)
Charles Tanford, Protein denaturation. C. Theoretical models for the mechanism of denaturation. Advances in Protein Chemistry. ,vol. 24, pp. 1- 95 ,(1970) , 10.1016/S0065-3233(08)60241-7
Moselio Schaechter, John L. Ingraham, Frederick C. Neidhardt, Physiology of the bacterial cell : a molecular approach Sinauer Associates. ,(1990)
Marcos E. Milla, Bronwen M. Brown, Robert T. Sauer, P22 Arc repressor: Enhanced expression of unstable mutants by addition of polar C‐terminal sequences Protein Science. ,vol. 2, pp. 2198- 2205 ,(1993) , 10.1002/PRO.5560021219
Mitchell S. Gittelman, C. Robert Matthews, Folding and stability of trp aporepressor from Escherichia coli. Biochemistry. ,vol. 29, pp. 7011- 7020 ,(1990) , 10.1021/BI00482A009
Thorlakur Jonsson, Carey D. Waldburger, Robert T. Sauer, Nonlinear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediates. Biochemistry. ,vol. 35, pp. 4795- 4802 ,(1996) , 10.1021/BI953056S
Bronwen M. Brown, Marcos E. Milla, Tracy L. Smith, Robert T. Sauer, Scanning mutagenesis of the Arc represser as a functional probe of operator recognition Nature Structural & Molecular Biology. ,vol. 1, pp. 164- 168 ,(1994) , 10.1038/NSB0394-164
Steven J. Metallo, Alanna Schepartz, Certain bZIP peptides bind DMA sequentially as monomers and dimerize on the DMA Nature Structural & Molecular Biology. ,vol. 4, pp. 115- 117 ,(1997) , 10.1038/NSB0297-115
Alexandre M.J.J. Bonvin, Hans Vis, Jan N. Breg, Maurits J.M. Burgering, Rolf Boelens, Robert Kaptein, Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations Journal of Molecular Biology. ,vol. 236, pp. 328- 341 ,(1994) , 10.1006/JMBI.1994.1138
Marcos E. Milla, Robert T. Sauer, P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. Biochemistry. ,vol. 33, pp. 1125- 1133 ,(1994) , 10.1021/BI00171A011
Jan N. Breg, Joost H. J. van Opheusden, Maurits J. M. Burgering, Rolf Boelens, Robert Kaptein, Structure of Arc represser in solution: evidence for a family of β-sheet DMA-binding proteins Nature. ,vol. 346, pp. 586- 589 ,(1990) , 10.1038/346586A0