【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020305563ZK.pdf | 164KB | download |