FEBS letters, 1998-02, Vol.423 (1), p.61-65
1998
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Details
- Autor(en) / Beteiligte
- Titel
- Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum
- Ist Teil von
- FEBS letters, 1998-02, Vol.423 (1), p.61-65
- Ort / Verlag
- England: Elsevier B.V
- Erscheinungsjahr
- 1998
- Quelle
- Wiley-Blackwell Journals
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1016/S0014-5793(98)00065-9Titel-ID: cdi_proquest_miscellaneous_79731685
- Format
- –
- Schlagworte
- Alanine - analogs & derivatives, Alanine - metabolism, Animals, 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), Cell Line, Cerebroside-Sulfatase - biosynthesis, Cerebroside-Sulfatase - genetics, Cerebroside-Sulfatase - metabolism, Chondro-4-Sulfatase - biosynthesis, Chondro-4-Sulfatase - genetics, Chondro-4-Sulfatase - metabolism, Cricetinae, Cysteine - genetics, Cysteine - metabolism, DNP, 2,4-dinitrophenyl, Endoplasmic reticulum, Endoplasmic Reticulum - metabolism, ER, endoplasmic reticulum, Eukaryotic Cells - metabolism, FGly, Cα-formylglycine, Glycine - analogs & derivatives, Glycine - metabolism, Humans, Multiple sulfatase deficiency, 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, Protein modification, Protein Processing, Post-Translational, Protein transport, RP-HPLC, reversed phase-high performance liquid chromatography, Sulfatase, Time Factors