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FEBS Lett. 2015 Jul 8;589(15):1802-6. doi: 10.1016/j.febslet.2015.05.032. Epub 2015 May 27.

The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation.

Author information

1
Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, Hans-Meerwein-Strasse 4, 35032 Marburg, Germany.
2
Department of Chemistry/Biochemistry, LOEWE Center for Synthetic Microbiology, Philipps-Universität Marburg, Hans-Meerwein-Strasse 4, 35032 Marburg, Germany. Electronic address: marahiel@staff.uni-marburg.de.

Abstract

Thurincin H is a 31-residue, ribosomally synthesized bacteriocin originating from the thn operon of Bacillus thuringiensis SF361. It is the only known sactipeptide carrying four thioether bridges between four cysteines and the α-carbons of a serine, an asparagine and two threonine residues. By analysis of the thn operon and use of in vitro studies we now reveal that ThnB is a radical S-adenosylmethionine (SAM) enzyme containing two [4Fe-4S] clusters. Furthermore, we confirm the involvement of ThnB in the formation of the thioether bonds present within the structure of thurincin H. Finally, we show that the PqqD homologous N-terminal domain of ThnB is essential for maturation of the thurincin H precursor peptide, but not for the SAM cleavage activity of ThnB.

KEYWORDS:

Biosynthesis; Natural product; Radical SAM enzyme; Ribosomal peptide; Sactipeptide; [4Fe–4S] cluster

PMID:
26026269
DOI:
10.1016/j.febslet.2015.05.032
[Indexed for MEDLINE]
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