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J. Bacteriol., Mar 1996, 1770-1773, Vol 178, No. 6
Copyright © 1996, American Society for Microbiology

SurA assists the folding of Escherichia coli outer membrane proteins

SW Lazar and R Kolter
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston MA 02115, USA.

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.


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