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J Biol Chem, Vol. 274, Issue 22, 15375-15381, May 28, 1999
From the Institut für Biochemie und Molekulare Zellbiologie,
Abteilung Biochemie II, Universität Göttingen,
Gosslerstrasse 12d, 37073 Göttingen, Germany
The catalytic residue of eukaryotic and
prokaryotic sulfatases is a 
-formylglycine. In the sulfatase of
Klebsiella pneumoniae the formylglycine is generated by
posttranslational oxidation of serine 72. We cloned the
atsBA operon of K. pneumoniae and found that
the sulfatase was expressed in inactive form in Escherichia coli transformed with the structural gene (atsA).
Coexpression of the atsB gene, however, led to production
of high sulfatase activity, indicating that the atsB gene
product plays a posttranslational role that is essential for the
sulfatase to gain its catalytic activity. This was verified after
purification of the sulfatase from the periplasm of the cells. Peptide
analysis of the protein expressed in the presence of AtsB revealed that
half of the polypeptides carried the formylglycine at position 72, while the remaining polypeptides carried the encoded serine. The
inactive sulfatase expressed in the absence of AtsB carried exclusively
serine 72, demonstrating that the atsB gene is required for
formylglycine modification. This gene encodes a 395-amino acid residue
iron sulfur protein that has a cytosolic localization and is supposed to directly or indirectly catalyze the oxidation of the serine to formylglycine.
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