Diverse Protein Architectures and α-N-Methylation Patterns Define Split Borosin RiPP Biosynthetic Gene Clusters.
Diverse Protein Architectures and α-N-Methylation Patterns Define Split Borosin RiPP Biosynthetic Gene Clusters.
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DOI：
10.1021/acschembio.1c01002
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发表时间：
2022-04-15
影响因子：
4
通讯作者：
Freeman, Michael F.
中科院分区：
文献类型：
--
作者：
Imani, Aman S.;Lee, Aileen R.;Vishwanathan, Nisha;de Waal, Floris;Freeman, Michael F.
Borosins 是核糖体合成的翻译后修饰肽 (RiPP)，肽主链上安装有 α-N-甲基化，赋予这些天然产物独特的性质，如蛋白水解稳定性。 Borosin RiPP 家族最初仅在真菌中被报道，直到我们最近在金属呼吸细菌 Shewanella oneidensis 中发现并表征了 IV 型分裂 borosin 系统。在这里，我们使用隐马尔可夫模型和序列相似性网络来识别 1600 多个假定途径，这些途径表明分裂的硼松素生物合成基因簇在细菌中广泛存在。前体和 α-N-甲基转移酶开放阅读框大小、结构和核心肽特性之间的显着差异允许将 borosin 家族进一步细分为六种额外的离散结构类型，其中五种已在本研究中得到验证。
Borosins are ribosomally synthesized and post-translationally modified peptides (RiPPs) with α-N-methylations installed on the peptide backbone that impart unique properties like proteolytic stability to these natural products. The borosin RiPP family was initially reported only in fungi until our recent discovery and characterization of a Type IV split borosin system in the metal-respiring bacterium Shewanella oneidensis. Here, we used hidden Markov models and sequence similarity networks to identify over 1600 putative pathways that show split borosin biosynthetic gene clusters are widespread in bacteria. Noteworthy differences in precursor and α-N-methyltransferase open reading frame sizes, architectures, and core peptide properties allow further subdivision of the borosin family into six additional discrete structural types, of which five have been validated in this study.
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