Kinetic analysis of operator binding by the E. coli methionine repressor highlights the role(s) of electrostatic interactions.

doi:10.1016/S0014-5793(04)00336-9

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Article

Kinetic analysis of operator binding by the E. coli methionine repressor highlights the role(s) of electrostatic interactions.

FEBS letters - 23 Apr 2004

Lawrenson Isobel D, Stockley Peter G

Abstract excerpt

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...

Topics

Bacterial Proteins
Biosensing Techniques
Escherichia coli Proteins
Kinetics
Mutagenesis, Site-Directed
Mutation
Operator Regions, Genetic
Protein Binding
Repressor Proteins
Salts
Static Electricity
Surface Plasmon Resonance

Source

Open in PubMed

Identifiers

PMID: 15094055
DOI: 10.1016/S0014-5793(04)00336-9

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