Escherichia coli exports previously folded and biotinated protein domains.

摘要: Biotination of proteins is a post-translational modification that requires folded acceptor domain. We previously showed an domain fused to the carboxyl terminus several cytosolic results in biotinated fusion vivo. now show encoded by translational gene fusions two periplasmic proteins, alkaline phosphatase and TEM beta-lactamase, carboxyl-terminal biotin-accepting sequences are exported Escherichia coli. Expression protein wild type strains resulted inefficient biotination product. This result was due rapid export before could occur since very large increase levels observed lacking SecB chaperone protein. The beta-lactamase but only stable DegP protease. Both accumulated culture medium possessing defective outer membranes. These indicate machinery can accommodate both into its mature conformation