N终端域对sHSPLo18函数的影响
Tiffany Bellanger1, Camille Eicher1, Fabien Garces1
1INRAE, UMR PAM, Institut Agro, Université de Bourgogne Europe, 21000, Dijon, France.
Scientific reports
|December 20, 2025
概括
小热冲击蛋白 (sHSP) Lo18的N端域对其寡合体结构和与蛋白质和脂质基质的相互作用至关重要,影响其伴侣和脂质伴侣功能.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 细胞应激反应的应激反应
背景情况:
- 外部压力会破坏细胞内部环境,导致蛋白质错折和膜损伤.
- 细胞利用热冲击蛋白 (HSP),包括小热冲击蛋白 (sHSP),以抵消压力引起的损伤.
- sHSPs具有保存的结构,具有α-晶域 (ACD) 和终端域,使其能够执行各种功能,如监护和 lipochaperoning.
研究的目的:
- 研究细菌sHSP Lo18.18的N端域的特定作用.
- 为了确定N端域对Lo18的寡合结构的影响,预防蛋白质聚合,以及保持膜流动性.
- 检查N端域在Lo18和细胞膜之间的相互作用中的参与.
主要方法:
- 对野生类型的Lo18和缺少N端27氨基酸的截断突变物的比较分析.
- 评估寡合体结构,抗聚合能力和膜流动性.
- 逆相高性能液态染色学 (RP-HPLC) 用于研究Lo18-膜相互作用.
主要成果:
- N端域对于Lo18寡合体的形成和稳定性至关重要.
- N端域显著影响Lo18与蛋白质和脂质基质的相互作用.
- 与野生类型相比,一个截断的Lo18蛋白质表现出受损的陪伴者和 lipochaperone 活动.
结论:
- sHSP Lo18的N端域是其结构完整性和功能活动的关键决定因素.
- 了解N端域在sHSPs中的作用,可以了解细胞应激反应机制.
- 这项研究强调了终端域在sHSP函数中超出保存的ACD之外的重要性.
相关概念视频
Conservation of Protein Domains Over Different Proteins
13.9K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.9K
Conserved Binding Sites
5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K
The JAK-STAT Signaling Pathway
11.7K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
11.7K
Regulation of Nuclear Protein Sorting
3.1K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.1K
Assembly of Signaling Complexes
6.4K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.4K
Energy to Drive Translocation
2.6K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
2.6K


