相关实验视频
Updated: Jun 13, 2025

09:16
Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
8.4K
控制PASTA激酶依赖ReoM酸化的细胞系因子
Patricia Rothe1, Sabrina Wamp1, Lisa Rosemeyer1
1FG11 Division of Enteropathogenic Bacteria and Legionella, Robert Koch Institute, Wernigerode, Germany.
Molecular microbiology
|September 8, 2024
概括
在Listeria monocytogenes中,GpsB激活PASTA激酶PrkA,控制ReoM酸化和MurA稳定性. 这种调节糖生物合成受到生长阶段和细胞内信号的影响.
科学领域:
- 微生物学 微生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 糖甘 (PG) 生物合成对于阳性细菌至关重要,PASTA 激酶调节这一过程.
- 激酶激活PASTA及其基质的机制,如ReoM,尚未完全理解.
- PrkA 的 ReoM 酸化影响了 MurA 的稳定性,这是PG 合成中的关键酶.
研究的目的:
- 为了阐明PASTA激酶PrkA激活在Listeria monocytogenes中的调节机制.
- 研究GpsB在PrkA信号传递和ReoM酸化中的作用.
- 了解生长阶段和MurA水平如何影响ReoM酸化.
主要方法:
- 对L. monocytogenes突变 (prkA,gpsB,MurA降解突变) 的遗传分析.
- 在体内分析ReoM酸化.
- 生物化学试验用于研究蛋白质相互作用和激酶激活.
主要成果:
- GpsB被确定为PrkA的激活剂,具有激活所需的特定结构特征.
- ReoM酸化依赖于生长阶段,并由酸酶PrpC.调节.
- 过度表达MurA抑制了ReoM酸化,这表明MurA和ReoM之间存在相互作用.
结论:
- GpsB是PrkA的关键激活剂,将细胞分裂与PG生物合成调节联系起来.
- ReoM酸化是一种由细胞内信号和生长阶段控制的动态过程.
- 这些发现扩大了对细菌中PASTA激酶激活和PG稳态的理解.
相关概念视频
Protein Kinases and Phosphatases
13.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.1K
Phosphorylation
50.1K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
50.1K
Calmodulin-dependent Signaling
5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
PI3K/mTOR/AKT Signaling Pathway
3.4K
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
3.4K
cAMP-dependent Protein Kinase Pathways
6.2K
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
6.2K
Amplifying Signals via Enzymatic Cascade
8.4K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
8.4K

