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小分子蛋白介导的铵转运抑制——古老的机制?

Small protein mediates inhibition of ammonium transport in -an ancient mechanism?

机构信息

Institut für allgemeine Mikrobiologie, Christian-Albrechts-Universität zu Kiel , Kiel, Germany.

Institute of Biocomputation and Physics of Complex Systems (BIFI), Universidad de Zaragoza , Zaragoza, Spain.

出版信息

Microbiol Spectr. 2023 Dec 12;11(6):e0281123. doi: 10.1128/spectrum.02811-23. Epub 2023 Nov 1.

Abstract

Small proteins containing fewer than 70 amino acids, which were previously disregarded due to computational prediction and biochemical detection challenges, have gained increased attention in the scientific community in recent years. However, the number of functionally characterized small proteins, especially in archaea, is still limited. Here, by using biochemical and genetic approaches, we demonstrate a crucial role of the small protein sP36 in the nitrogen metabolism of , which modulates the ammonium transporter AmtB1 according to nitrogen availability. This modulation might represent an ancient archaeal mechanism of AmtB1 inhibition, in contrast to the well-studied uridylylation-dependent regulation in bacteria.

摘要

近年来,科学界对以前由于计算预测和生化检测挑战而被忽视的小蛋白(含少于 70 个氨基酸的蛋白质)给予了更多关注。然而,功能表征的小蛋白数量,尤其是在古菌中,仍然有限。在这里,我们通过生化和遗传方法证明了小蛋白 sP36 在 氮代谢中的关键作用,它根据氮的可用性调节铵转运体 AmtB1。这种调节可能代表了一种古老的古菌 AmtB1 抑制机制,与细菌中研究充分的尿苷酰化依赖性调节机制形成对比。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df95/10714827/8aa91f44560e/spectrum.02811-23.f001.jpg

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