Functional identification of the SecB homologue in Methanococcus jannaschii and direct interaction of SecB with trigger factor.

In this study Mj0357 protein, a hypothetical protein from Methanococcus jannaschii which shows an 18% sequence identity with SecB from E. coli, has been identified as a functional homologue of SecB in M. jannaschii through a number of biochemical and biophysical examinations. It is composed mostly of beta-strands and exists as a homotetramer in solution. Mj0357 protein exhibits in vitro chaperone-like activity, suppressing thermal aggregation of citrate synthase and binding to partially folded maltose-binding protein. Upon binding to a peptide ligand, the protein undergoes a conformational change to expose a hydrophobic patch on the protein surface. All these physicochemical properties are highly similar to those of E. coli SecB. In addition, E. coli trigger factor (TF) has been shown here for the first time to bind E. coli SecB and Mj0357 protein with low micromolar affinities, indicating that the TF could interact directly along the SecB-dependent translocation pathway. These results indicate that the translocation pathway is conserved and functionally homologous in at least one of the archaeal organisms.