Cooper, A., Mcalpine, A. and Stockley, P. G. (1994) Calorimetric studies of the energetics of protein—DNA interactions in the E. coli methionine repressor (MetJ) system. FEBS Letters, 348(1), pp. 41-45. (doi: 10.1016/0014-5793(94)00579-6)
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Publisher's URL: http://dx.doi.org/10.1016/0014-5793(94)00579-6
Abstract
Calorimetric measurements of binding of a specific DNA fragment and <i>S</i>-adenosyl methionine (SAM) co-repressor molecules to the <i>E. Coli</i> methionine repressor (MetJ) show significant differences in the energetics of binary and ternary protein-DNA complexes. Formation of the MetJ: SAM: DNA ternary complex is significantly more exothermic (ΔH ⋍ −99 kJ•mol<sup>−1</sup>) than either MetJ:DNA or MetJ:SAM binary complexes alone (ΔH ⋍ −10 kJ•mol<sup>−1</sup> each). The protein is also significantly more stable to unfolding (ΔT<sub>m</sub> ⋍ 5.4°C) when bound to DNA. These observations suggest that binding of SAM to the protein-DNA complex leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropy-enthalpy compensation, not necessarily involving any overall conformational change.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Cooper, Professor Alan |
| Authors: | Cooper, A., Mcalpine, A., and Stockley, P. G. |
| Subjects: | Q Science > QH Natural history > QH345 Biochemistry |
| College/School: | College of Science and Engineering > School of Chemistry |
| Journal Name: | FEBS Letters |
| Publisher: | Elsevier BV |
| ISSN: | 0014-5793 |
| ISSN (Online): | 1873-3468 |
| Published Online: | 19 October 2001 |
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