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相关概念视频

Protein Modifications in the RER01:26

Protein Modifications in the RER

5.1K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

5.7K
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...
5.7K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

6.7K
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.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
6.7K
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

5.7K
Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
5.7K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.2K
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...
7.2K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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相关实验视频

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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

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米血清水氧甲基转移酶:进化,亚细胞定位,功能和前景.

Tian Pan1, Hongmiao Jin1, Chuanhui Zhou1

  • 1The Key Laboratory for Quality Improvement of Agricultural Products of Zhejiang Province, College of Advanced Agricultural Sciences, Zhejiang A&F University, Hangzhou 311300, China.

Plants (Basel, Switzerland)
|April 27, 2024
PubMed
概括
此摘要是机器生成的。

这项研究全面分析了大米氨酸氧甲基转移酶 (SHMT) 基因,揭示了单种植物中的基因损失和OsSHMT3.3的意外叶绿体局部化. 这些SHMT可能在应激反应中发挥作用.

关键词:
功能 功能 功能 功能.米 米饭 米饭 米饭 米饭.氨酸氧甲基转移酶 (Serine Hydroxymethyltransferase) 是一种酶.

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科学领域:

  • 植物分子生物学 植物分子生物学
  • 基因家族分析 基因家族分析
  • 米的遗传学 米的遗传学

背景情况:

  • 对于米中氨酸氧甲基转移酶 (SHMT) 基因家族成员的功能研究有限.
  • 了解SHMT功能对于植物发育和应激反应至关重要.

研究的目的:

  • 对大米SHMT基因家族进行全面调查.
  • 阐明OSSHMTs的遗传学关系,基因结构,表达模式,亚细胞定位和蛋白质相互作用.

主要方法:

  • 人类遗传学分析
  • 基因结构和促进体分析
  • 表达方式的分析.
  • 亚细胞局部化试验 (大米原生质)
  • 蛋白质与蛋白质相互作用研究 (二分化试验)

主要成果:

  • 鉴定了一种基因丢失事件在单类动物内的质细胞局部化组IIaSHMTs中.
  • OsSHMT3,最初被归类为细胞质,被局部化为叶绿体.
  • 所有五个OsSHMT都形成了同质体;OsSHMT3与其他OsSHMT (除了OsSHMT1) 具有独特的二元化,这表明它具有移动和协作作用.
  • 预测的cis-acting元素和表达数据表明OsSHMT家族参与压力和激素调节.

结论:

  • OsSHMT3表现出独特的局部化和二元化特性,可能作为质体中的移动蛋白.
  • 米中的OsSHMT家族涉及到各种应激反应和激素信号通路.
  • 这项研究为未来对植物中SHMT功能的研究提供了基础的见解.