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

Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Research Abstract Details 

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Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Abstract Text:

T Dierks,B Schmidt,K von Figura,T Dierks,B Schmidt,K von Figura,

In sulfatases a Calpha-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 Calpha-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.

Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Publishing Authors By Initials

T Dierks,B Schmidt,K von Figura,T Dierks,B Schmidt,K von Figura,

For similar genetic processes: gene expression regulation: protein modification, translational: protein processing, post-translational research abstracts see: genetic processes: gene expression regulation: protein modification, translational: protein processing, post-translational research

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Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 94

Page Numbers: 11963-8

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 28

MONTH: Oct

YEAR: 1997

Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Information

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LANGUAGE: eng

NlmUniqueID: 7505876

Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Keywords Mesh Terms:

KEYWORDS: Protein Processing, Post-Translational

MESH TERMS: enzymology

Chemical & Substance for Abstract: Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Information

Substance Name: Cerebroside-Sulfatase

Registry Number: EC 3.1.6.8

Grant and Affiliation Information for Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum.

AFFILIATION: Institut für Biochemie und Molekulare Zellbiologie, Abteilung Biochemie II, Universität Göttingen, Gosslerstrasse 12d, 37073 Göttingen, Germany.

Country: UNITED STATES

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MEDLINETA: Proc Natl Acad Sci U S A

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Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum Related Publications

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• Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum.
• ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum.
• Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme.
• Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.
• Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine.
• Residues critical for formylglycine formation and/or catalytic activity of arylsulfatase A.
• Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases.
• Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine.
• The Non-catalytic N-terminal Extension of Formylglycine-generating Enzyme Is Required for Its Biological Activity and Retention in the Endoplasmic Reticulum.
• The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes.