来自Bordetella pertussis的周周等离子体结合蛋白Bug69和Bug27在体外是高亲和度林酸结合剂,在NAD生物合成中可能发挥作用

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Leonardo Sorci¹, Gabriele Minazzato², Adolfo Amici³

¹Division of Bioinformatics and Biochemistry, Department of Science and Engineering of Matter, Environment and Urban Planning, Polytechnic University of Marche, Ancona, Italy.

|August 9, 2024

概括

波德泰拉虫,特别是Bug27和Bug69,与关键的NAD前体诺酸结合. 这一发现将这些未分配的蛋白与细菌中必不可少的NAD代谢联系起来.

科学领域:

微生物学微生物学
生物化学生物化学
基因组学就是基因组学.

背景情况:

波德特拉拥有众多未表征的周等离子体结合蛋白 (PBPs),称为Bugs.
之前假设Bug27和Bug69可以运输用于NAD生物合成的氨酸前体.

研究的目的:

为了研究Bug27和Bug69的特定联结能力.
为了阐明Bug27和Bug69在Bordetella的代谢途径中的功能作用.

主要方法:

在体外结合试验测试以确定连接物亲和力.
序列相似性网络和基因组上下文分析.
分子对接和基于结构的对齐.

主要成果:

布格27和布格69表现出对酸的高亲和度结合 (微米级范围).
奎诺酸是优选的配体,而不是其他NAD前体.
Bug69/27的同类基因组与NAD代谢基因 (NadQ,nadC) 有关.

结论:

布格27和布格69的功能是作为林酸的运输体.
这些发现确立了昆虫与Bordetella中的NAD生物合成之间的直接联系.
这项研究赋予了以前未被描述的细菌蛋白的功能.

关键词:

波尔代特拉吸收基因的基因在NAD生物合成过程中.分子对接的分子对接.周等离子体结合蛋白质化酸的化转移酶可以转移酸.序列相似性网络是一个序列相似性网络.

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