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在Salmonella Typhimurium和Bacillus subtilis中,核蛋白相关的HU蛋白是N-终端乙化

Anastacia R Parks¹, Jessica L Will¹, Liju G Mathew¹

¹Department of Microbiology, University of Georgia, Athens, GA 30602, USA.

Pathogens (Basel, Switzerland)

|July 30, 2025

概括

沙门氏菌 Typhimurium NatB 乙化物与核相关的 HU 蛋白. 这种乙化对HU功能至关重要,并且由甲氨酸硫氧化减少酶逆转,表明它在氧化应激反应中的作用.

科学领域:

微生物学微生物学
分子生物学分子生物学
蛋白质生物化学蛋白质生物化学

背景情况:

像HU这样的核素相关蛋白质对于细菌的DNA组织和基因调节至关重要.
N-终端乙化是一种常见的翻译后修饰,但它在细菌HU蛋白中的作用尚未完全理解.
氧化应激会影响蛋白质功能,需要细胞修复机制.

研究的目的:

通过NatB复合体来研究沙门氏菌Typhimurium HU蛋白的N端乙化.
确定HU乙化对转录调节的功能影响.
探索HU乙化,甲胺氧化和氧化应激反应之间的相互作用.

主要方法:

在体外乙化试验中使用与沙门氏菌Typhimurium NatB (SeNatB) 净化的HUα,HUβ和 lysine-null 变种进行了试验.
在体内研究,检查乙化对HU介导的hilA促进体调节的影响.
在甲氨酸氧化和随后使用甲氨酸硫氧化还原酶 (MsrA和MsrB) 进行减少后对HU蛋白的乙化分析.
细菌细菌YfmK作为SeNatB.的同类的功能性表征.

主要成果:

SeNatB直接乙化沙门氏菌HU蛋白的N终端氨酸.
通过SeNatB对HU蛋白的乙化影响了hilA促进体的转录调节.
SeNatB不会对HU蛋白质上的氧化氨酸残留物进行乙化,但通过MsrA/MsrB进行减少会恢复乙化.
细菌亚细菌YfmK作为SeNatB的同类物,使细菌亚细菌HU (HBsu) 的N终端甲酸化.

结论:

沙门氏菌的HU蛋白是SeNatB对N端乙化的基质,影响基因表达.
HU乙化和甲氨酸氧化/减少之间的相互作用表明,甲氨酸在控制氧化应激方面起着作用.
细菌的N-终端乙化通路,如涉及NatB和YfmK的,被保存,并在蛋白质功能和细胞调节中发挥重要作用.

关键词:

格拉姆阴性细菌是一种细菌.格拉姆阳性细菌是什么?这是一种HU蛋白,HU蛋白.在N端的乙化.沙门菌的病原性后翻译修改后的修改.蛋白质乙转移酶是一种蛋白质乙转移酶.

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