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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Abstract
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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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.
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56 Citations in Europe PMC

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Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency.
Meshach Paul D, Chadah T, Senthilkumar B, Sethumadhavan R, Rajasekaran R., J. Biomol. Struct. Dyn. (), 2017
PMID: 29048999
Comparative study of idursulfase beta and idursulfase in vitro and in vivo.
Kim C, Seo J, Chung Y, Ji HJ, Lee J, Sohn J, Lee B, Jo EC., J. Hum. Genet. 62(2), 2017
PMID: 27829684
Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction.
Peng J, Alam S, Radhakrishnan K, Mariappan M, Rudolph MG, May C, Dierks T, von Figura K, Schmidt B., FEBS J. 282(17), 2015
PMID: 26077311

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