Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum

FEBS Letters

von Figura, Kurt¹  Dierks, Thomas¹  Schmidt, Bernhard¹  Lecca, Maria Rita¹ 

[1] Institut für Biochemie und Molekulare Zellbiologie, Abt. Biochemie II, Universität Göttingen, Gosslerstr. 12d, 37073 Göttingen, Germany

关键词: Sulfatase;    Endoplasmic reticulum;    Protein modification;    Protein transport;    Multiple sulfatase deficiency;    ASA;    arylsulfatase A (cerebroside-3-sulfate 3-sulfohydrolase;    EC 3.1.6.8);    ASB;    arylsulfatase B (N-acetylgalactosamine-4-sulfate 4-sulfohydrolase;    EC 3.1.6.9);    DNP;    2;    4-dinitrophenyl;    ER;    endoplasmic reticulum;    FGly;    Cα-formylglycine;    P3;    cysteine-containing form of tryptic peptide 3 of ASB;    P3*;    FGly-containing form of tryptic peptide 3 of ASB;    P3C;    C-terminal fragment of P3 generated by endopeptidase AspN;    P3*C;    C-terminal fragment of P3* generated by endopeptidase AspN;    RP-HPLC;    reversed phase-high performance liquid chromatography;   

DOI  :  10.1016/S0014-5793(98)00065-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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