title: A model for heterooligomer formation in the heat shock response of Escherichia coli.
abstract: Small heat shock proteins (sHsp) are widely distributed molecular chaperones that bind to misfolded proteins to prevent irreversible aggregation and aid in refolding to a competent state. The sHsps characterized thus far all contain a conserved α-crystallin, and variable N- and C-termini critical for chaperone activity and oligomerization. The Escherichia coli sHsps IbpA and IbpB share 48% sequence homology, are induced by heat shock and oxidative stress, and each requires the presence of the other to effect protein protection. Molecular Dynamics (MD) simulations of homology-modeled monomers and heterooligomers of these sHsps identify a possible mechanism for cooperation between IbpA and IbpB.
authors.affiliation: Department of Chemistry, St. Edward's University, Austin, TX 78704, USA. healy@stedwards.edu
authors.forename: Eamonn F
authors.initials: EF
authors.lastname: Healy
mesh_terms: D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D018869:Heat-Shock Response; D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C097578:IbpA protein, E coli; C097579:IbpB protein, E coli