Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum

Fey J, Balleininger M, Borissenko LV, Schmidt B, Figura von K, Dierks T (2001)
JOURNAL OF BIOLOGICAL CHEMISTRY 276(50): 47021-47028.

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Abstract
C-alpha-formylglycine is the key catalytic residue in the active site of sulfatases. In eukaryotes formylglycine is generated during or immediately after sulfatase translocation into the endoplasmic reticulum by oxidation of a specific cysteine residue. We established an in vitro assay that allowed us to measure formylglycine modification independent of protein translocation. The modifying enzyme was recovered in a microsomal detergent extract. As a substrate we used ribosome-associated nascent chain complexes comprising in vitro synthesized sulfatase fragments that were released from the ribosomes by puromycin. Formylglycine modification was highly efficient and did not require a signal sequence in the substrate polypeptide. Ribosome association helped to maintain the modification competence of nascent chains but only after their release efficient modification occurred. The modifying machinery consists of soluble components of the endoplasmic reticulum lumen, as shown by differential extraction of microsomes. The in vitro assay can be performed under kinetically controlled conditions. The activation energy for formylglycine formation is 61 kJ/mol, and the pH optimum is approximate to 10. The activity is sensitive to the SH/SS equilibrium and is stimulated by Ca2+. Formylglycine formation is efficiently inhibited by a synthetic sulfatase peptide representing the sequence directing formylglycine modification. The established assay system should make possible the biochemical identification of the modifying enzyme.
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Fey J, Balleininger M, Borissenko LV, Schmidt B, Figura von K, Dierks T. Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. JOURNAL OF BIOLOGICAL CHEMISTRY. 2001;276(50):47021-47028.
Fey, J., Balleininger, M., Borissenko, L. V., Schmidt, B., Figura von, K., & Dierks, T. (2001). Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. JOURNAL OF BIOLOGICAL CHEMISTRY, 276(50), 47021-47028.
Fey, J., Balleininger, M., Borissenko, L. V., Schmidt, B., Figura von, K., and Dierks, T. (2001). Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. JOURNAL OF BIOLOGICAL CHEMISTRY 276, 47021-47028.
Fey, J., et al., 2001. Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. JOURNAL OF BIOLOGICAL CHEMISTRY, 276(50), p 47021-47028.
J. Fey, et al., “Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 276, 2001, pp. 47021-47028.
Fey, J., Balleininger, M., Borissenko, L.V., Schmidt, B., Figura von, K., Dierks, T.: Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. JOURNAL OF BIOLOGICAL CHEMISTRY. 276, 47021-47028 (2001).
Fey, J, Balleininger, M, Borissenko, LV, Schmidt, B, Figura von, K, and Dierks, Thomas. “Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum”. JOURNAL OF BIOLOGICAL CHEMISTRY 276.50 (2001): 47021-47028.
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15 Citations in Europe PMC

Data provided by Europe PubMed Central.

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SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency.
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A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.
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Recent insight on the control of enzymes involved in estrogen formation and transformation in human breast cancer.
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The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases.
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Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.
Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K., Cell 113(4), 2003
PMID: 12757705

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