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Title

Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal
Authors
Monnat, J
Hacker, U
Geissler, H
Rauchenberger, R
Neuhaus, E M
Maniak, M
Soldati, Thierry
Published in FEBS Letters. 1997, vol. 418, no. 3, p. 357-62
Abstract 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 Ca2+ 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.
Keywords Amino Acid Sequence — Animals — Cloning, Molecular — Dictyostelium/enzymology/genetics/ultrastructure — Endoplasmic Reticulum/enzymology — Molecular Sequence Data — Protein Disulfide-Isomerases/genetics/metabolism — Sequence Alignment — Sequence Analysis
Identifiers
PMID: 9428745
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(ISO format) 		MONNAT, J et al. Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal. In: FEBS Letters, 1997, vol. 418, n° 3, p. 357-62. https://archive-ouverte.unige.ch/unige:18930

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