| Autor: |
Enoru-Eta J; Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussels, Belgium., Gigot D, Glansdorff N, Charlier D |
| Jazyk: |
angličtina |
| Zdroj: |
Molecular microbiology [Mol Microbiol] 2002 Sep; Vol. 45 (6), pp. 1541-55. |
| DOI: |
10.1046/j.1365-2958.2002.03136.x |
| Abstrakt: |
Ss-Lrp, from Sulfolobus solfataricus, is an archaeal homologue of the global bacterial regulator Lrp (Leucine-responsive regulatory protein), which out of all genome-encoded proteins is most similar to Escherichia coli Lrp (E-value of 5.6 e-14). The recombinant protein has been purified as a 68 kDa homotetramer. The specific binding of Ss-Lrp to its own control region is suggestive of negative autoregulation. A high resolution contact map of Ss-Lrp binding was established by DNase I and hydroxyl radical footprinting, small non-intercalating groove-specific ligand-binding interference, and various base-specific premodification and base removal binding interference techniques. We show that Ss-Lrp binds one face of the DNA helix and establishes the most salient contacts with two major groove segments and the intervening minor groove, in a region that overlaps the TATA-box and BRE promoter elements. Therefore, Ss-Lrp most likely exerts autoregulation by preventing promoter recognition by TBP and TFB. Moreover, the results demonstrate profound Ss-Lrp induced structural alterations of sequence stretches flanking the core contact site, and reveal that the deformability of these regions significantly contributes to binding selectivity. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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