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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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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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.
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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Espejo-Mojica AJ, Almeciga-Diaz CJ, Rodriguez A, Mosquera A, Diaz D, Beltran L, Diaz S, Pimentel N, Moreno J, Sanchez J, Sanchez OF, Cordoba H, Poutou-Pinales RA, Barrera LA., Mol. Genet. Metab. 116(1-2), 2015
PMID: 26071627
Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry.
Navare AT, Chavez JD, Zheng C, Weisbrod CR, Eng JK, Siehnel R, Singh PK, Manoil C, Bruce JE., Structure 23(4), 2015
PMID: 25800553
Radical S-adenosylmethionine enzymes.
Broderick JB, Duffus BR, Duschene KS, Shepard EM., Chem. Rev. 114(8), 2014
PMID: 24476342
Microbial alkyl- and aryl-sulfatases: mechanism, occurrence, screening and stereoselectivities.
Toesch M, Schober M, Faber K., Appl. Microbiol. Biotechnol. 98(4), 2014
PMID: 24352732
High-density transcriptional initiation signals underline genomic islands in bacteria.
Huang Q, Cheng X, Cheung MK, Kiselev SS, Ozoline ON, Kwan HS., PLoS ONE 7(3), 2012
PMID: 22448273
Sulfotransferases, sulfatases and formylglycine-generating enzymes: a sulfation fascination.
Bojarova P, Williams SJ., Curr Opin Chem Biol 12(5), 2008
PMID: 18625336
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.
Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ., Biochemistry 47(28), 2008
PMID: 18558715
Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes.
Benjdia A, Subramanian S, Leprince J, Vaudry H, Johnson MK, Berteau O., J. Biol. Chem. 283(26), 2008
PMID: 18408004
Systemic inflammation and neurodegeneration in a mouse model of multiple sulfatase deficiency.
Settembre C, Annunziata I, Spampanato C, Zarcone D, Cobellis G, Nusco E, Zito E, Tacchetti C, Cosma MP, Ballabio A., Proc. Natl. Acad. Sci. U.S.A. 104(11), 2007
PMID: 17360554
Carbonylation of milk powder proteins as a consequence of processing conditions.
Fenaille F, Parisod V, Tabet JC, Guy PA., Proteomics 5(12), 2005
PMID: 16038017
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, von Figura K, Ficner R, Rudolph MG., Cell 121(4), 2005
PMID: 15907468
Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility.
Hanson SR, Best MD, Wong CH., Angew. Chem. Int. Ed. Engl. 43(43), 2004
PMID: 15493058

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