Journal
FEBS LETTERS
Volume 564, Issue 1-2, Pages 136-142Publisher
WILEY
DOI: 10.1016/S0014-5793(04)00336-9
Keywords
methionine repressor; operator binding; surface plasmon resonance; Escherichia coli
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MetJ is a member of the ribbon-helix-helix class of DNA-binding proteins whose affinity for operators is apparently controlled by an unprecedented long-range electrostatic effect from the tertiary sulphur atom of its co-repressor, S-adenosyl methionine. We report here the results of kinetic assays of DNA binding with MetJ mutant proteins having altered net charges. The results (a) suggest that MetJ locates its operators via a sliding mechanism, (b) support the idea that electrostatic steering is important in the initial DNA binding event and (c) highlight the sensitivity of this system to electrostatic effects. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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