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首页> 外文期刊>Applied Microbiology >ε-Poly-l-Lysine Peptide Chain Length Regulated by the Linkers Connecting the Transmembrane Domains of ε-Poly-l-Lysine Synthetase
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ε-Poly-l-Lysine Peptide Chain Length Regulated by the Linkers Connecting the Transmembrane Domains of ε-Poly-l-Lysine Synthetase

机译：ε-聚赖氨酸肽链的长度受连接ε-聚赖氨酸合成酶跨膜结构域的接头调控

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摘要

ε-Poly-l-lysine (ε-PL), consisting of 25 to 35 l-lysine residues with linkages between the α-carboxyl groups and ε-amino groups, is produced by Streptomyces albulus NBRC14147. ε-PL synthetase (Pls) is a membrane protein with six transmembrane domains (TM1 to TM6) as well as both an adenylation domain and a thiolation domain, characteristic of the nonribosomal peptide synthetases. Pls directly generates ε-PL chain length diversity (25- to 35-mer), but the processes that control the chain length of ε-PL during the polymerization reaction are still not fully understood. Here, we report on the identification of Pls amino acid residues involved in the regulation of the ε-PL chain length. From approximately 12,000 variants generated by random mutagenesis, we found 8 Pls variants that produced shorter chains of ε-PL. These variants have one or more mutations in two linker regions connecting the TM1 and TM2 domains and the TM3 and TM4 domains. In the Pls catalytic mechanism, the growing chain of ε-PL is not tethered to the enzyme, implying that the enzyme must hold the growing chain until the polymerization reaction is complete. Our findings reveal that the linker regions are important contributors to grasp the growing chain of ε-PL.
机译：链霉菌NBRC14147产生ε-聚-1-赖氨酸（ε-PL），该残基由25至35个l-赖氨酸残基组成，在α-羧基和ε-氨基之间具有连接键。 ε-PL合成酶（Pls）是具有六个跨膜结构域（TM1至TM6）以及非核糖体肽合成酶特征的腺苷酸化域和硫醇化域的膜蛋白。 Pls直接产生ε-PL链长的多样性（25-35-mer），但是在聚合反应过程中控制ε-PL链长的方法仍不完全清楚。在这里，我们报道了参与调控ε-PL链长度的Pls氨基酸残基的鉴定。从随机诱变产生的大约12,000个变体中，我们发现了8个Pls变体，它们产生了较短的ε-PL链。这些变体在连接TM1和TM2结构域以及TM3和TM4结构域的两个接头区域中具有一个或多个突变。在P1s催化机理中，ε-PL的增长链没有束缚在酶上，这意味着酶必须保持该增长链，直到聚合反应完成。我们的发现表明，连接子区域是掌握ε-PL增长链的重要贡献者。

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