Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.

ABSTRACT: The central region of the LacI N-subdomain monomer-monomer interface includes residues K84, V94, V95, V96, S97, and M98. The side chains of these residues line the β-strands at this interface and interact to create a network of hydrophobic, charged, and polar interactions that significantly rearranges in different functional states of LacI. Prior work showed that converting K84 to an apolar residue or converting V96 to an acidic residue impedes the allosteric response to inducer. Thus, we postulated that a disproportionate number of substitutions in this region of the monomer-monomer interface would alter the complex features of the LacI allosteric response. To explore this hypothesis, acidic, basic, polar, and apolar mutations were introduced at positions 94-98. Despite their varied locat

SUBMITTER: Zhan H 

PROVIDER: S-EPMC3006071 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature