SurA assists the folding of Escherichia coli outer membrane proteins

作者：Sara W. Lazar, Roberto Kolter · 发表于：Journal of Bacteriology · 年份：1996 · DOI：10.1128/jb.178.6.1770-1773.1996 · 被引用次数：331 · 研究领域：Signaling Pathways in Disease、Lipid Membrane Structure and Behavior、Toxin Mechanisms and Immunotoxins

Many proteins require enzymatic assistance in order to achieve a functional conformation. One rate-limiting step in protein folding is the cis-trans isomerization of prolyl residues, a reaction catalyzed by prolyl isomerases. SurA, a periplasmic protein of Escherichia coli, has sequence similarity with the prolyl isomerase parvulin. We tested whether SurA was involved in folding periplasmic and outer membrane proteins by using trypsin sensitivity as an assay for protein conformation. We determined that the efficient folding of three outer membrane proteins (OmpA, OmpF, and LamB) requires SurA in vivo, while the folding of four periplasmic proteins was independent of SurA. We conclude that SurA assists in the folding of certain secreted proteins.