PMID:15094055

Citation	Lawrenson, ID and Stockley, PG (2004) Kinetic analysis of operator binding by the E. coli methionine repressor highlights the role(s) of electrostatic interactions. FEBS Lett. 564:136-42
Abstract	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.
Links	PubMed Online version:10.1016/S0014-5793(04)00336-9
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Biosensing Techniques; Escherichia coli Proteins/genetics; Kinetics; Mutagenesis, Site-Directed; Mutation; Operator Regions, Genetic; Protein Binding; Repressor Proteins/chemistry; Repressor Proteins/genetics; Salts/pharmacology; Static Electricity; Surface Plasmon Resonance
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