关于Synechococcus sp. 的MoxR AAA+ ATPase的分子表征 菌株NKBG15041c是一种
Kota Mano1, Kentaro Noi1, Kumiko Oe1
1Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.
International journal of molecular sciences
|September 28, 2024
概括
我们发现了一种新型的耐压基因,SyMRP,来自Synechococcus. 这种MoxR AAA+ ATPase表现出依赖ATP的伴侣活性和独特的六合体结构,提供对细胞应激的保护.
科学领域:
- 微生物学 微生物学
- 分子生物学分子生物学
- 生物化学 生化学
背景情况:
- 耐压力对微生物生存至关重要.
- AAA+ ATPases 是各种细胞过程中必不可少的分子机器.
- 这种病原体是Synechococcus sp. NKBG15041c是一种以其弹性而闻名的蓝藻细菌.
研究的目的:
- 为了隔离和表征一种在Synechococcus中赋予耐压力的基因.
- 为了研究已识别的蛋白质的生物化学和结构性质,SyMRP.
- 阐明通过SyMRP调解的应力保护机制.
主要方法:
- 来自Synechococcus sp.的基因分离 NKBG15041c的基因组图书馆.
- 在大肠杆菌中异质表达和功能分析.
- 生物化学测定ATPase和伴侣活动.
- 使用分析超离心 (AUC),小角度X射线散射 (SAXS),原子力显微镜 (AFM) 和传输电子显微镜 (TEM) 的结构分析.
- 使用AlphaFold 3进行in silico结构预测.
主要成果:
- 一个新型基因,被指定为SyMRP,编码MoxR AAA+ ATPase,被分离出来,在大肠杆菌表达时赋予了抗压力.
- 再组合的SyMRP表现出较弱的ATPase活性,并以ATP依赖的方式保护酸盐合成酶免受热聚合.
- SyMRP形成了一个稳定的六合体,但结构分析 (AFM,TEM,SAXS) 显示了一个非正规的环结构,与AlphaFold 3的预测不同.
- 在六米结构中没有检测到依赖ATP的构造变化.
结论:
- SyMRP是一种新型的耐压因子,具有依赖ATP的伴侣活性.
- 赛姆RP具有独特的,非正规的六合体结构,与典型的AAA+ ATPases不同.
- 需要进一步的结构和功能研究来充分理解SyMRP在应激反应中的机制.
更多相关视频
12:29Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
2.2K
12:23Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
7.5K
相关概念视频
ATP Synthase: Mechanism
14.0K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
14.0K
ATP Synthase: Structure
11.9K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
11.9K
