微蛋白转入新阶段:定义未定义的
Aayushi Sahgal1, Vladimir Uversky2, Vrushank Davé3
1Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, United States; Biotechnology Graduate Program, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, United States.
Methods (San Diego, Calif.)
|October 27, 2023
概括
新发现的微蛋白 (miP) 很小,但在生物学上很强大,会影响细胞功能和疾病. 这项研究描述了它们的结构和功能,揭示了它们在液-液相分离和细胞分离中的作用.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 奥米克技术已经确定了微蛋白 (miPs),这是一种新型的短聚类.
- 尽管尺寸小,miP表现出重要的生物功能,影响细胞生理和疾病.
- miPs可以通过近,近和内分泌信号通路发挥作用.
研究的目的:
- 进行生物化学和生物物理分析,对24个人类毫秒进行分析.
- 为了阐明miPs的结构特征和物理化学特性.
- 调查miPs在液体液相分离 (LLPS) 和细胞内凝结物形成中的作用.
主要方法:
- 使用了计算方法,包括RIDAO,AlphaFold2,D2P2,FuzDrop,STRING和Emboss Pep轮.
- 分析了被选中的人类miPs的物理化学性质和结构特征.
- 评估了miP对液态液态相分离 (LLPS) 的倾向.
主要成果:
- 描述了24个人类的物理化学特性和结构景观.
- 证明miPs可以驱动或参与液态-液态相分离 (LLPS) 并形成细胞内凝结物.
- 确定了特定的miP,如NoBody和pTUNAR,对LLPS的倾向很高,这表明它们参与了无膜有机体的形成.
结论:
- 微蛋白 (miPs) 具有不寻常的结构性质和重要的生物功能.
- miPs在细胞分隔和信号传递中起着至关重要的作用,对于正常的细胞功能至关重要.
- 了解miP的行为对于开发针对性治疗miP相关疾病至关重要.
相关概念视频
Bacterial Protein Maturation
22
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
22
Translocation of Proteins into the Mitochondria
3.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
Positive Regulator Molecules
106.2K
To consistently produce healthy cells, the cell cycle—the process that generates daughter cells—must be precisely regulated.
106.2K
Post-translational Translocation of Proteins to the RER
5.7K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
5.7K
Proteomics
7.4K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.4K
Mitochondrial Precursor Proteins
2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
Most of the mitochondrial...
2.6K


