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Scientific article
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Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal

Published inFEBS letters, vol. 418, no. 3, p. 357-362
Publication date1997
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
Affiliation Not a UNIGE publication
Citation (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. 357–362. doi: 10.1016/s0014-5793(97)01415-4
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ISSN of the journal0014-5793
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