细胞内乙酸调节大肠杆菌的 pyruvate 代谢
Ling Zhang1,2, Hongmei Shi3, Zixiang Liu1,2
1Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Acta biochimica et biophysica Sinica
|May 15, 2025
概括
这项研究揭示了酸乙烯 (AcP) 如何在大肠杆菌中修改酸盐脱酶 (AceE),影响酸盐代谢. 通过AcP介导的乙化和脱乙化调节酶活性和细菌代谢途径.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 微生物学 微生物学
背景情况:
- 氨酸乙化是细菌中一个关键的翻译后修饰,使用乙酸 (AcP) 作为乙捐赠体.
- 酸盐脱酶 (PDH) 复合体对于将酸盐转化为乙烯-CoA至关重要,将碳水化合物代谢联系起来.
- lysine 乙化和 pyruvate 代谢之间的相互作用,特别是涉及 AcP 和 PDH,仍然未被充分研究.
研究的目的:
- 调查乙酸 (AcP) 在Escherichia coli pyruvate dehydrogenase (AceE) 的酸乙化中的作用.
- 阐明AcP介导的ACE乙化对其酶活性和大肠杆菌中酸盐的整体代谢的影响.
- 建立AcP,蛋白质乙化和中央代谢途径调节之间的直接联系.
主要方法:
- 在体外和体内实验,以评估在大肠杆菌中ACEE的AcP介导的乙化.
- 酶活性测定测量乙化和酸化对ACE功能的影响.
- 基因删除研究 (ackA,pta) 分析对AceE活性,乙化水平和酸盐代谢的影响.
- 通过CobB介导的脱乙化实验来确认ACE乙化过程的可逆性.
主要成果:
- 乙酸 (AcP) 已被证明在体外和体内直接乙化大肠杆菌AceE,这是CobB.的可逆修饰.
- 在体外对AceE的AcP治疗导致酸化增加和酶活性降低.
- 删除ackA导致AceE乙化和活性增加,而pta删除减少了这两种.
- 在pta删除突变体和ackA突变体中观察到pyruvate积累,这些突变体也表现出pyruvate代谢基因 (ldhA,poxB) 的改变表达.
结论:
- 细胞内乙酸盐 (AcP) 通过乙化甲酸脱酶 (AceE) 直接调节大肠杆菌中的酸盐代谢.
- 通过AcP介导的AceE的lysine乙化会影响其酶活性和酸化状态.
- 这项研究确立了AcP依赖蛋白质乙化,酸盐脱酶调节和细菌中酸盐代谢的控制之间的新鲜联系.
更多相关视频
08:07Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
Published on: July 26, 2019
8.5K
11:08A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
6.8K
相关概念视频
Phosphorylation
49.5K
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...
49.5K
Protein Kinases and Phosphatases
12.9K
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...
12.9K
Phosphoinositides and PIPs
7.3K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
7.3K
Covalently Linked Protein Regulators
6.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.7K
Calmodulin-dependent Signaling
5.0K
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,...
5.0K
Cholinergic Neurons: Neurotransmission
2.5K
Cholinergic neurotransmission involves the synthesis and the release of acetylcholine (ACh) in order to transmit nerve impulses across the synapse. The process begins with the synthesis of acetyl CoA, a precursor for ACh, from ATP, acetate, and coenzyme A in the mitochondria. Choline, another vital precursor, is transported inside the neuron through choline transporters, including high-affinity choline transporter CHT1, low-affinity choline transporter CTL1, and lower-affinity choline...
2.5K
