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J. Biol. Chem., Vol. 278, Issue 4, 2212-2218, January 24, 2003

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Posttranslational Modification of Serine to Formylglycine in Bacterial Sulfatases
RECOGNITION OF THE MODIFICATION MOTIF BY THE IRON-SULFUR PROTEIN AtsB^*

Claudia Marquordt, Qinghua Fang, Elke Will, Jianhe Peng, Kurt von Figura, and Thomas Dierks^§

From the Institut für Biochemie und Molekulare Zellbiologie, Abt. Biochemie II, Universität Göttingen, Heinrich-Düker-Weg 12, 37073 Göttingen, Germany and  Abteilung für Molekulare Genetik, Max-Planck-Institut für Biophysikalische Chemie, 37070 Göttingen, Germany

C-formylglycine is the catalytic residue of sulfatases. Formylglycine is generated by posttranslational modification of a cysteine (pro- and eukaryotes) or serine (prokaryotes) located in a conserved (C/S)XPXR motif. The modifying enzymes are unknown. AtsB, an iron-sulfur protein, is strictly required for modification of Ser⁷² in the periplasmic sulfatase AtsA of Klebsiella pneumoniae. Here we show (i) 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 Ser⁷²-dependent manner, as shown in yeast two-hybrid and GST pull-down 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.

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