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          Institute: MPI für biophysikalische Chemie     Collection: Ehemalige Abteilungen     Display Documents

ID: 17169.0, MPI für biophysikalische Chemie / Ehemalige Abteilungen
Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB
Authors:Marquordt, C.; Fang, Q. H.; Will, E.; Peng, J. H.; von Figura, K.; Dierks, T.
Date of Publication (YYYY-MM-DD):2003-01-24
Title of Journal:Journal of Biological Chemistry
Issue / Number:4
Start Page:2212
End Page:2218
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Calpha-formylglycine is the catalytic residue of sulfatases. Formylglycine is generated by posttranslational modification of a cysteine (pro- and eukaryotes) or serine (pro-karyotes) located in a conserved (C/S)XPXR motif. The modifying enzymes are unknown. AtsB, an iron-sulfur protein, is strictly required for modification of Se-72 in the periplasmic sulfatase AtsA of Klebsiella pneumoniae. Here we show W that AtsB is a cytosolic protein acting on newly synthesized serine-type sulfatases, (ii) that AtsB-mediated FGly formation is dependent on AtsA's signal peptide, and (iii) that the cytosolic cysteine-type sulfatase of Pseudomonas aeruginosa can be converted into a substrate of AtsB if the cysteine is substituted by serine and a signal peptide is added. Thus, formylglycine formation in serine-type sulfatases depends both on AtsB and on the presence of a signal peptide, and AtsB can act on sulfatases of other species. AtsB physically interacts with AtsA in a Ser(72)- dependent manner, as shown in yeast two-hybrid and GST pulldown experiments. This strongly suggests that AtsB is the serine- modifying enzyme and that AtsB relies on a cytosolic function of the sulfatase's signal peptide.
Comment of the Author/Creator:Date: 2003, JAN 24
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Dieter Gallwitz / 150
External Affiliations:Univ Gottingen, Inst Biochem & Mol Zellbiol, Biochem Abt 2,; Henrich Duker Weg 12, D-37073 Gottingen, Germany; Univ Gottingen, Inst Biochem & Mol Zellbiol, Biochem Abt 2, D-37073 Gottingen, Germany
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