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Journal Article

Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB

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Will,  E.
Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society;

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Peng,  J. H.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Citation

Marquordt, C., Fang, Q. H., Will, E., Peng, J. H., von Figura, K., & Dierks, T. (2003). Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB. Journal of Biological Chemistry, 278(4), 2212-2218. Retrieved from http://www.jbc.org/content/278/4/2212.full.pdf+html.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F18F-F
Abstract
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.