Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB

Fang QH, Peng JH, Dierks T (2004)
JOURNAL OF BIOLOGICAL CHEMISTRY 279(15): 14570-14578.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Fang, QH; Peng, JH; Dierks, ThomasUniBi
Einrichtung
Fakultät für Chemie > Biochemie I
Abstract / Bemerkung
C-alpha-Formylglycine (FGly) is the catalytic residue of sulfatases. FGly is generated by post-translational modification of a cysteine ( prokaryotes and eukaryotes) or serine ( prokaryotes) located in a conserved (C/S) XPXR motif. AtsB of Klebsiella pneumoniae is directly involved in FGly generation from serine. AtsB is predicted to belong to the newly discovered radical S-adenosylmethionine (SAM) superfamily. By in vivo and in vitro studies we show that SAM is the critical co-factor for formation of a functional AtsB . SAM . sulfatase complex and for FGly formation by AtsB. The SAM-binding site of AtsB involves (83)GGE(85) and possibly also a juxtaposed FeS center coordinated by Cys(39) and Cys(42), as indicated by alanine scanning mutagenesis. Mutation of these and other conserved cysteines as well as treatment with metal chelators fully impaired FGly formation, indicating that all three predicted FeS centers are crucial for AtsB function. It is concluded that AtsB oxidizes serine to FGly by a radical mechanism that is initiated through reductive cleavage of SAM, thereby generating the highly oxidizing deoxyadenosyl radical, which abstracts a hydrogen from the serine-CbetaH2-OH side chain.
Erscheinungsjahr
2004
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
279
Ausgabe
15
Seite(n)
14570-14578
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/2350732

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Fang QH, Peng JH, Dierks T. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY. 2004;279(15):14570-14578.
Fang, Q. H., Peng, J. H., & Dierks, T. (2004). Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY, 279(15), 14570-14578. https://doi.org/10.1074/jbc.M313855200
Fang, QH, Peng, JH, and Dierks, Thomas. 2004. “Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB”. JOURNAL OF BIOLOGICAL CHEMISTRY 279 (15): 14570-14578.
Fang, Q. H., Peng, J. H., and Dierks, T. (2004). Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY 279, 14570-14578.
Fang, Q.H., Peng, J.H., & Dierks, T., 2004. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY, 279(15), p 14570-14578.
Q.H. Fang, J.H. Peng, and T. Dierks, “Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 279, 2004, pp. 14570-14578.
Fang, Q.H., Peng, J.H., Dierks, T.: Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY. 279, 14570-14578 (2004).
Fang, QH, Peng, JH, and Dierks, Thomas. “Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB”. JOURNAL OF BIOLOGICAL CHEMISTRY 279.15 (2004): 14570-14578.

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