在Thermococcus kodakarensis中,SmsB-SmsC机器作为一个古老的支架,介导Fe-S集群组件
Jian-Qiang Jin1, Takaaki Sato1,2, Haruyuki Atomi1,2
1Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto, Japan.
Applied and environmental microbiology
|August 18, 2025
概括
来自Thermococcus kodakarensis的SUF类最小系统 (SMS),包括Tk-SmsB和Tk-SmsC,成功地产生和转移铁硫. 这一发现支持SMS作为广泛保存的SUF系统的原始祖先.
科学领域:
- 生物化学 生物化学
- 微生物学 微生物学
- 分子生物学分子生物学
背景情况:
- 铁硫 (Fe-S) 集群对于许多生物过程至关重要.
- SUF系统是细菌和真核生物体中Fe-S集群生物发生的关键机制.
- 缺乏 SufD 的 SUF 类最小系统 (SMS) 被提出为祖先的 Fe-S 集群组装支架.
研究的目的:
- 为了研究来自高热友的考古体Thermococcus kodakarensis的候选SMS蛋白 (Tk-SmsB和Tk-SmsC) 的功能.
- 确定Tk-SmsB和Tk-SmsC是否可以调解Fe-S集群生成和传输.
- 探索SMS和SUF系统之间的进化关系.
主要方法:
- 对Tk-SmsB和Tk-SmsC复合物的生化表征.
- 测试Tk-SmsC ATPase活性及其通过复杂形成的调制.
- 通过Tk-SmsB2C2复合体使用铁和硫化物离子展示Fe-S集群生成.
- 铁-S集群转移试验对阿波-基合成酶 (LipS).
- 使用囊氨酸作为硫供体生成Fe-S集群和LipS激活.
主要成果:
- Tk-SmsB和Tk-SmsC形成了一个稳定的异质四重体Tk-SmsB2C2复合体.
- Tk-SmsC表现出ATPase活性,在与Tk-SmsB.复合形成时得到增强.
- Tk-SmsB2C2复合体有效地产生了Fe-S集群,并将其转移到apo-LipS,恢复其活动.
- 囊脱硫酶和ATP使得apo-Tk-SmsB2C2复合物能够产生Fe-S集群并激活LipS.
结论:
- 在Tk-SmsB和Tk-SmsC中,它们作为Thermococcus kodakarensis中Fe-S集群生物发生的SMS支架.
- 这种古老的SMS系统能够进行Fe-S集群合成和转移,支持其在原始Fe-S集群组装中的作用.
- 这些发现为SMS作为各种生命形式中发现的SUF系统的进化前体提供了进一步的证据.
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