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

Marquordt C, Fang QH, Will E, Peng JH, Figura von K, Dierks T (2003)
JOURNAL OF BIOLOGICAL CHEMISTRY 278(4): 2212-2218.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
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.
Erscheinungsjahr
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
278
Zeitschriftennummer
4
Seite
2212-2218
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Marquordt C, Fang QH, Will E, Peng JH, Figura von K, Dierks T. Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY. 2003;278(4):2212-2218.
Marquordt, C., Fang, Q. H., Will, E., Peng, J. H., Figura von, 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. doi:10.1074/jbc.M209435200
Marquordt, C., Fang, Q. H., Will, E., Peng, J. H., Figura von, K., and 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, 2212-2218.
Marquordt, C., et al., 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), p 2212-2218.
C. Marquordt, et al., “Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 278, 2003, pp. 2212-2218.
Marquordt, C., Fang, Q.H., Will, E., Peng, J.H., Figura von, K., Dierks, T.: 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, 2212-2218 (2003).
Marquordt, C, Fang, QH, Will, E, Peng, JH, Figura von, K, and Dierks, Thomas. “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 (2003): 2212-2218.

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