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对子SAMD9的结构和功能研究揭示了一个独特的tRNase模块,它是抗病毒活性的基础

Juhi Chaturvedi¹, Fushun Zhang², Chen Zhang²

¹Department of Biochemistry and Molecular biology, Oklahoma State University, Stillwater, Oklahoma, United States of America.

|July 31, 2025

概括

形SAMD9蛋白质保留了抗病毒和蛋白质合成调节功能,尽管关键的残留物变化. 这种蛋白质利用扩展的tRNase模块来准氨酸tRNA (tRNAPhe).

科学领域:

分子生物学分子生物学
病毒学病毒学
结构生物学结构生物学

背景情况:

SAMD9/9L蛋白质是蛋白质合成的关键调节者,并具有抗病毒性质.
人类SAMD9 (hSAMD9) 酶活性依赖于其tRNase域内的特定基本残留物.
拉哥摩尔夫SAMD9 (rSAMD9) 呈现出一种独特的电荷逆转酸性残留物,与保存的哺乳动物 ортолог不同.

研究的目的:

调查 SAMD9 (rSAMD9) 与其抗病毒活性和tRNA耗尽有关的功能和结构特征.
了解与人类SAMD9.9相比,形动物SAMD9的独特残留变异如何影响其生物功能.

主要方法:

功能性比较试验评估疫苗病毒限制和tRNAPhe耗尽由rSAMD9.9.
生物化学分析以确定rSAMD9.9的最小tRNase模块.
确定rSAMD9 tRNase域的晶体结构.

主要成果:

子SAMD9 (rSAMD9) 有效地限制了疫苗病毒的复制,并消耗了tRNAPhe,类似于hSAMD9.
rSAMD9的功能性tRNase模块比hSAMD9更大,包括SIR2区域.
额外的基本残留物,包括一个对rSAMD9独特的残留物,对其抗病毒活性至关重要.
rSAMD9的tRNase域的晶体结构与hSAMD9具有结构上的相似性,但具有不同的循环形状.

结论:

拉哥形SAMD9保持了重要的tRNA向和抗病毒功能,尽管有显著的残留物改变.
扩展的tRNase模块和额外的基本残留物有助于rSAMD9的功能活动.
结构和功能上的分歧凸显了SAMD9/9L蛋白质的进化适应性.

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