Ss-LrpB from Sulfolobus solfataricus condenses about 100 base pairs of its own operator DNA into globular nucleoprotein complexes

The Journal of Biological Chemistry
Eveline PeetersDaniel Charlier

Abstract

Ss-LrpB from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2 is a member of the Lrp-like family of Bacterial/Archaeal transcription regulators that binds its own control region at three regularly spaced and partially conserved 15-bp-long imperfect palindromes. We have used atomic force microscopy to analyze the architecture of Ss-LrpB.DNA complexes with a different stoichiometry formed with the wild type operator and with an operator mutant. Binding of dimeric Ss-LrpB to all three target sites is accompanied by the formation of globular complexes, in which the protein induces strong DNA deformations. Furthermore, DNA contour length foreshortening of these complexes indicates DNA wrapping, with about 100 bp being condensed. The average bending angle is 260 degrees . The establishment of protein-protein contacts between Ss-LrpB dimers in these globular complexes will contribute to the cooperativity of the binding. The profound remodeling of the control region is expected to have a strong impact on gene expression and might constitute the key element in the autoregulatory process.

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Citations

Feb 9, 2010·Nature Reviews. Microbiology·Shane C Dillon, Charles J Dorman
Jan 29, 2013·Nucleic Acids Research·Ningning SongDaniel Charlier
Feb 12, 2008·Journal of Bacteriology·Elizabeth A KarrJohn N Reeve
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Jul 16, 2020·Cells·Oleg V BylinoYulii V Shidlovskii

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