The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
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DOI：
10.1016/j.febslet.2015.05.032
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发表时间：
2015-07
期刊：
影响因子：
3.5
通讯作者：
Beata M Wieckowski;J. Hegemann;A. Mielcarek;Linda Boss;O. Burghaus;M. Marahiel
中科院分区：
文献类型：
--
作者：
Beata M Wieckowski;J. Hegemann;A. Mielcarek;Linda Boss;O. Burghaus;M. Marahiel
Thurincin H 是一种由 31 个残基核糖体合成的细菌素，源自苏云金芽孢杆菌 SF361 的 thethnoperon。它是唯一已知的在四个半胱氨酸与丝氨酸、天冬酰胺和两个苏氨酸残基的α-碳之间携带四个硫醚桥的硫肽。通过对thnoperon的分析和体外研究，我们现在揭示ThnB是一种自由基S-腺苷甲硫氨酸（SAM）酶，含有两个[4Fe-4S]簇。此外，我们证实了ThnB参与了苏打素H结构中存在的硫醚键的形成。最后，我们表明ThnB的PqqD同源N端结构域对于苏打素H前体肽的成熟是必需的，但对于ThnB的SAM裂解活性不是必需的。
Thurincin H is a 31-residue, ribosomally synthesized bacteriocin originating from thethnoperon ofBacillus thuringiensisSF361. 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 thethnoperon and use of in vitro studies we now reveal that ThnB is a radicalS-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 homologousN-terminal domain of ThnB is essential for maturation of the thurincin H precursor peptide, but not for the SAM cleavage activity of ThnB.