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Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL‐type retrieval signal
Author(s) -
Monnat Jean,
Hacker Ulrike,
Geissler Heidrun,
Rauchenberger Robert,
Neuhaus Eva M.,
Maniak Markus,
Soldati Thierry
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01415-4
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , dictyostelium discoideum , kdel , biochemistry , foldase , enzyme , signal peptide , isomerase , microbiology and biotechnology , biology , er retention , chemistry , peptide sequence , gene , mutant , escherichia coli , groel , golgi apparatus
The primary activity of protein disulfide isomerase (PDI), a multifunctional resident of the endoplasmic reticulum (ER), is the isomerization of disulfide bridges during protein folding. We isolated a cDNA encoding Dictyostelium discoideum PDI (Dd‐PDI). Phylogenetic analyses and basic biochemical properties indicate that it belongs to a subfamily called P5, many members of which differ from the classical PDIs in many respects. They lack an intervening inactive thioredoxin module, a C‐terminal acidic domain involved in Ca 2+ binding and a KDEL‐type retrieval signal. Despite the absence of this motif, the ER is the steady‐state location of Dd‐PDI, suggesting the existence of an alternative retention mechanism for P5‐related enzymes.