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Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum

By Thomas Dierks, Bernhard Schmidt and Kurt von Figura

Abstract

In sulfatases a C(α)-formylglycine residue is found at a position where their cDNA sequences predict a cysteine residue. In multiple sulfatase deficiency, an inherited lysosomal storage disorder, catalytically inactive sulfatases are synthesized which retain the cysteine residue, indicating that the C(α)-formylglycine residue is required for sulfatase activity. Using in vitro translation in the absence or presence of transport competent microsomes we found that newly synthesized sulfatase polypeptides carry a cysteine residue and that the oxidation of its thiol group to an aldehyde is catalyzed in the endoplasmic reticulum. A linear sequence of 16 residues surrounding the Cys-69 in arylsulfatase A is sufficient to direct the oxidation. This novel protein modification occurs after or at a late stage of cotranslational protein translocation into the endoplasmic reticulum when the polypeptide is not yet folded to its native structure

Topics: Biological Sciences
Publisher: The National Academy of Sciences of the USA
Year: 1997
DOI identifier: 10.1073/pnas.94.22.11963
OAI identifier: oai:pubmedcentral.nih.gov:23670
Provided by: PubMed Central
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