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Mutational and functional analysis of the E. coli molecular chaperone, DnaJ, in the recognition of a lambda nucleoprotein complex

Initiation of λ phage replication involves a series of sequential steps leading to the formation of a pre‐replication complex (preRC) on λ DNA. However, replication can not proceed until this multimeric complex, composed of λO, λP and the E. coli DNA replicative helicase, DnaB, is recognized and subsequently remodeled by the molecular chaperones DnaJ and DnaK. Little is known about the mechanism by which the chaperones mediate the reorganization of this complex. Evidence indicates that DnaJ first recognizes the preRC and recruits DnaK through the stimulation of DnaK's intrinsic ATPase activity. This leads to partial disassembly of the preRC and subsequent loading of DnaB onto DNA. Unfortunately, the stoichiometry of the DnaJ:preRC binding reaction as well as the site(s) of their interaction remain enigmatic.