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相关概念视频

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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tRNA Activation02:26

tRNA Activation

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Leaky Scanning02:28

Leaky Scanning

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
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Tail-anchoring of Proteins in the ER Membrane01:45

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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...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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相关实验视频

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Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
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Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions

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在YTH域外的ECT2序列调节其m6A-RNA结合.

Daphné Seigneurin-Berny1, Claire Karczewski1, Elise Delaforge2

  • 1Université Grenoble Alpes, INSERM U 1209, CNRS UMR 5309, Institut pour l'Avancée des Biosciences, Grenoble, France.

RNA biology
|September 13, 2024
PubMed
概括

这项研究揭示了ECT2蛋白中控制其与m6A甲基化RNA结合的新型调节区域,扩大了我们对真核细胞表转录组调节的理解.

关键词:
阿拉比多普西斯塔利亚纳.美国EMSA的EMSA是EMSA.这是一个IDR IDR.有关RNA结合的RNA.YTH 域名域名这是一种YTH蛋白质.m6A 一个很好的.

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
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科学领域:

  • 分子生物学分子生物学
  • 遗传学 是一个遗传学.
  • 生物化学 生物化学

背景情况:

  • N6-甲基氨酸 (m6A) 是一种普遍存在的RNA修饰,对真核生物基因表达至关重要.
  • YTH域蛋白是m6A修饰的关键读者,但它们的调节机制尚未完全理解.
  • 在YTH蛋白中的内在无序区域 (IDR),如Arabidopsis thaliana的ECT2,与功能专业化有关.

研究的目的:

  • 生物化学描述ECT2蛋白的m6A结合特性.
  • 为了确定影响m6A结合的YTH域外的监管区域.
  • 调查增强ECT2对m6A修饰RNA的选择性因素.

主要方法:

  • 在体外生化表征全长ECT2及其YTH域.
  • 对m6A甲基化RNA结合亲和力和特异性的分析.
  • 调节性区和结构元素的识别.

主要成果:

  • 全长ECT2及其YTH域表现出明显的m6A结合能力.
  • ECT2的N端IDR区域调节其与m6A甲基化RNA的结合.
  • 通过侧面的富含尿素的序列来增强ECT2的m6A结合选择性.
  • 在YTH域附近保存的结构元素进一步增强了m6A结合.

结论:

  • 在YTH域外的新型监管区域控制ECT2的m6ARNA结合.
  • 尿素含量和特定的结构元素调节ECT2的结合亲和力和选择性.
  • 这些调节机制可能在真核YTH读者中保持.