在大肠杆菌中,蛋白质聚合驱动细胞衰老以特定大小的方式Escherichia coli
Linda Wagener1, Arpita Nath1, Murat Tuğrul1
1Freie Universität Berlin, Institute of Biology, Berlin, Germany.
mBio
|December 16, 2025
概括
细菌衰老与蛋白质聚合物的积累有关. 大肠杆菌的生长衰退是由总体的总量决定的.
科学领域:
- 细胞衰老和衰老的发生.
- 微生物学和细菌生理学
- 进化生物学和权衡问题
背景情况:
- 衰老涉及到受损组件的细胞内积累.
- 父母损伤的保留和后代的再生发生在各种物种中,包括像大肠杆菌这样的细菌.
- 关于蛋白质聚合物的健康影响,存在相互矛盾的证据.
研究的目的:
- 调查衰老大肠杆菌增长衰退的主要驱动因素.
- 量化单细胞细菌系中的损害积累和分离动态.
- 探索细胞大小调节作为抗衰老细菌中补偿机制的作用.
主要方法:
- 利用微流体设备在几代人中培养和跟踪单细胞大肠杆菌血统.
- 采用光标记的DnaK伴侣来监测细胞内损伤和聚合物形成.
- 量化总体大小,细胞内空间占用和细胞生长率.
主要成果:
- 大肠杆菌的细胞生长下降与蛋白质聚合物占据的细胞内空间直接相关,而不仅仅是它们的存在.
- 随着时间的推移,蛋白质总体直径线性增加,而母细胞逐渐扩大以适应损伤.
- 母细胞和子细胞之间出现了形态不对称性,这是由于差异性聚合物分裂和细胞扩大.
结论:
- 损伤所占的细胞内空间,而不是仅仅存在,决定了老化细菌的健康状况下降.
- 细胞膨胀在衰老的细菌中起到补偿机制的作用,尽管积累了损伤,但允许持续增长.
- 细菌衰老与真核细胞衰老具有相似之处,特别是在细胞大小调节方面,但在细菌中具有保护作用.
相关概念视频
Amyloid Fibrils
11.5K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
11.5K
Bacterial Protein Maturation
419
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...
419
Molecular Chaperones and Protein Folding
19.5K
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...
19.5K
Regulated Protein Degradation
8.7K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.7K
Stringent Response in E. coli
265
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
265
The Proteasome
1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K


