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Beteiligte Max-Planck-Institute |
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MPI für biophysikalische Chemie |
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Autoren |
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Marquordt, C.; Fang, Q. H.; Will, E.; Peng, J. H.; von Figura, K.; Dierks, T.; |
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Publikationstyp |
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Artikel |
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Titel |
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Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB |
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Zusammenfassung |
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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. |
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Quelle |
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Journal of Biological Chemistry 278 (4), 2212-2218 (2003) |
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Sprache |
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English |
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Identifikation |
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ISI 000180562000020
ISSN 0021-9258 |
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© 2009, Max-Planck-Gesellschaft, München |
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