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Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum
Author(s) -
Dierks Thomas,
Lecca Maria Rita,
Schmidt Bernhard,
von Figura Kurt
Publication year - 1998
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(98)00065-9
Subject(s) - endoplasmic reticulum , cysteine , biochemistry , chemistry , subcellular localization , arylsulfatase a , microbiology and biotechnology , enzyme , cytoplasm , biology
Sulfatases undergo an unusual protein modification leading to conversion of a specific cysteine residue into α‐formylglycine. This conversion is essential for catalytic activity. In arylsulfatase A the α‐formylglycine is generated inside the endoplasmic reticulum at a late stage of protein translocation. Using in vitro translation in the presence of transport‐competent microsomes we found that arylsulfatase B is also modified in a similar way by the formylglycine‐generating machinery. Modification depended on protein transport and on the correct position of the relevant cysteine. Arylsulfatase A and B did not compete for modification, as became apparent in co‐expression experiments. This could argue for an association of the modification machinery with the protein translocation apparatus.