迟衰失序蛋白的螺旋性有助于其在干燥过程中的保护功能
Sourav Biswas1, Edith Gollub2,3, Feng Yu2,3
1Department of Molecular Biology, University of Wyoming, Laramie, Wyoming, USA.
Protein science : a publication of the Protein Society
|December 19, 2023
概括
内在无序蛋白 (IDP) 在极度干燥期间有助于生存. 这项研究显示了迟衰CAHS D蛋白质的螺旋结构.
科学领域:
- 生物化学 生化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 有机体使用内在无序蛋白质 (IDP) 进行无水生态 (耐干燥).
- 过渡螺旋结构在IDP中对干燥耐受性的作用已被假设,但缺乏直接的经验证据.
研究的目的:
- 调查CAHS D蛋白中螺旋结构的必要性和充分性,以调解无水生态.
- 探索蛋白质结构,特别是螺旋性和干燥保护能力之间的关系.
主要方法:
- 通过引入螺旋分解残留物 (proline) 和改变氨基酸成分 (带电残留物,对血清素/甘氨酸有疏水性) 来改造CAHS D蛋白的工程变体.
- 评估野生类型CAHS D及其变体的螺旋内容.
- 将这些变体在干燥过程中的保护能力与其测量的螺旋含量相关联.
主要成果:
- 具有螺旋结构的CAHS D的链接区域被确定为保护域.
- 具有扰乱螺旋结构的变体显示出不同程度的干燥耐受性.
- 虽然螺旋体含量与保护相关,但这种关系不是绝对的,表明其他因素有助于无水生菌病.
结论:
- 提供了直接的实验证据,支持长期以来的理论,将IDP中的螺旋性与它们的无水生物功能联系起来.
- 表明,虽然螺旋性是关键因素,但它并不是由IDPs介导的干燥耐受性的唯一决定因素.
- 突出了内部流离失所者的结构特征的复杂相互作用,使其在极端环境条件下生存.
相关概念视频
02:18Intrinsically Disordered Proteins
17.9K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.9K
03:00Molecular Chaperones and Protein Folding
18.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.0K
01:28Protein Denaturation
4.2K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
4.2K
01:25Protein Folding
8.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.0K
01:32Export of Misfolded Proteins out of the ER
3.6K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.6K
02:45Responses to Heat and Cold Stress
13.5K
Every organism has an optimum temperature range within which healthy growth and physiological functioning can occur. At the ends of this range, there will be a minimum and maximum temperature that interrupt biological processes.
13.5K