相关实验视频

Updated: Jul 5, 2025

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells

Published on: January 7, 2019

PRMT-7/PRMT7激活HLH-30/TFEB,以保护由细菌孔形成毒素破坏的血膜完整性

Hui-Chen Hsieh^1,2, I-Hsiang Huang¹, Shao-Wen Chang¹

¹Department of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.

|January 23, 2024

概括

蛋白质氨酸甲基转移酶-7 (PRMT-7) 激活HLH-30/TFEB,这是对细菌毛孔形成毒素 (PFTs) 的细胞防御. 这种甲基化促进了核的进入,保护了宿主血的完整性,无论是虫还是人类.

科学领域:

细胞生物学细胞生物学
分子生物学分子生物学
病原体与宿主之间的相互作用

背景情况:

细菌孔形成毒素 (PFTs) 是关键的毒性因素,危害宿主血完整性 (PMI).
由HLH-30/TFEB介导的内在细胞防御 (INCED) 途径保护*C. elegans*中肠道上皮质免受PFTs的影响. 然而,PFTs激活HLH-30/TFEB的确切机制尚不清楚.

研究的目的:

阐明PFTs完全激活HLH-30/TFEB的分子机制.
为了识别参与PFT诱导的膜损伤的内在细胞防御的宿主因素.
为了研究这种防御机制的进化保存.

主要方法:

使用*C. elegans*模型研究PFT与宿主相互作用和HLH-30激活.
采用生物化学分析来评估蛋白质甲基化和核定位.
在人类肠道细胞系中验证的发现证实了进化保存.

主要成果:

确定了PRMT-7 (蛋白质氨酸甲基转移酶-7) 对于PFT诱导的HLH-30核转位和激活至关重要.
证明PRMT-7在其RAG复合体结合域上甲基化HLH-30,促进其进入核.
表明人类的PRMT7正义基因在调节TFEB局部化和修复PFT诱导的血损伤方面得到保护.

结论:

通过甲基化揭示了PRMT-7/PRMT7对HLH-30/TFEB的新型后翻译调节.
已确立的PRMT-7/PRMT7是进化保守的INCED路径中对甲基动物中PFTs的关键组成部分.
提供了对维持血膜完整性对抗细菌毒素的宿主策略的见解.

关键词:

内在的细胞防御 (INCED)血膜完整性 (PMI) 的研究.形成毛孔的毒素 (PFT)蛋白质氨酸甲基转移酶-7 (PRMT7/PRMT-7) 是一种转录因子EB (TFEB/HLH-30) 是一种转录因子.

更多相关视频

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

相关概念视频

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

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...

Tail-anchoring of Proteins in the ER Membrane

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

Transcription Attenuation in Prokaryotes

Transcription Attenuation in Prokaryotes

Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure. Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
There are several different mechanisms used to attenuate transcription. In ribosome mediated...

The Unfolded Protein Response

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

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...

Structure of Porins

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...