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J. Biol. Chem., Vol. 267, Issue 11, 7211-7214, 04, 1992
K Vuori, R Myllyla, T Pihlajaniemi and KI Kivirikko
Protein disulfide isomerase (PDI, EC 5.3.4.1) is a highly unusual
multifunctional polypeptide, being identical to the beta subunit of prolyl
4-hydroxylase, a cellular thyroid hormone binding protein and a component
of the microsomal triglyceride transfer protein complex, and highly similar
to a polypeptide acting in vitro as a glycosylation site binding protein.
It has two -Cys-Gly-His-Cys- sequences which, it has been proposed, act as
catalytic sites for the isomerase activity, but few data have been
available to indicate whether one or both of them do indeed act as
catalytic sites and whether the two presumed catalytic sites act
independently or cooperatively. We report here on the expression of human
PDI in Escherichia coli with three different signal sequences. All three
polypeptide variants were secreted into the periplasmic space as fully
active enzymes. Oligonucleotide-directed mutagenesis was used to convert
either one or both of the -Cys-Gly-His- Cys- sequences to
-Ser-Gly-His-Cys-. The PDI activity of both polypeptides containing a
single modified sequence was about 50% of that of the wild-type
polypeptide, whereas the polypeptide with two modified sequences had no
isomerase activity. It is thus concluded that both -Cys-Gly-His-Cys-
sequences act as catalytic sites for the isomerase activity, and the two
catalytic sites appear to operate independently of one another.
Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity
Collagen Research Unit, University of Oulu, Finland.
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