Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum

Dierks T, Schmidt B, VonFigura K (1997)
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 94(22): 11963-11968.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
In sulfatases a C-alpha-formylglycine residue is found at a position where their cDNA sequences predict a cysteine residue. In multiple sulfatase deficiency, an inherited lysosomal storage disorder, catalytically inactive sulfatases are synthesized which retain the cysteine residue, indicating that the C,-formylglycine residue is required for sulfatase activity. Using in vitro translation in the absence or presence of transport competent microsomes we found that newly synthesized sulfatase polypeptides carry a cysteine residue and that the oxidation of its thiol group to an aldehyde is catalyzed in the endoplasmic reticulum. A linear sequence of 16 residues surrounding the Cys-69 in arylsulfatase A is sufficient to direct the oxidation, This novel protein modification occurs after or at a late stage of cotranslational protein translocation into the endoplasmic reticulum when the polypeptide is not yet folded to its native structure.
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Zeitschriftentitel
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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94
Zeitschriftennummer
22
Seite
11963-11968
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Dierks T, Schmidt B, VonFigura K. Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1997;94(22):11963-11968.
Dierks, T., Schmidt, B., & VonFigura, K. (1997). Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 94(22), 11963-11968. doi:10.1073/pnas.94.22.11963
Dierks, T., Schmidt, B., and VonFigura, K. (1997). Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 94, 11963-11968.
Dierks, T., Schmidt, B., & VonFigura, K., 1997. Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 94(22), p 11963-11968.
T. Dierks, B. Schmidt, and K. VonFigura, “Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum”, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 94, 1997, pp. 11963-11968.
Dierks, T., Schmidt, B., VonFigura, K.: Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 94, 11963-11968 (1997).
Dierks, Thomas, Schmidt, B, and VonFigura, K. “Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 94.22 (1997): 11963-11968.

57 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Novel cofactors via post-translational modifications of enzyme active sites.
Okeley NM, van der Donk WA., Chem Biol 7(7), 2000
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Pathologic findings of multiple sulfatase deficiency reflect the pattern of enzyme deficiencies.
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