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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.9K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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2.9K
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
6.9K
Conserved Binding Sites01:49

Conserved Binding Sites

5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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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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Homologous Recombination02:31

Homologous Recombination

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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Updated: Feb 19, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
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遺伝子ナビゲーションを導くために,本質的に無秩序な領域をエンジニアリングする.

Jing Liu1, Divya Krishna Kumar1, Bohdana Hurieva1

  • 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.

Molecular cell
|February 17, 2026
PubMed
まとめ
この要約は機械生成です。

本質的に乱れた領域 (IDRs) は,特異転写因子 (TFs) を特定のDNA部位に誘導する. 新しい de novo IDR が設計され,調節可能なゲノム結合を直接制御することが示され,配列でコードされた認識の原理が明らかになりました.

キーワード:
ChEC-seqq について遺伝子調節 遺伝子調節本質的に無秩序な地域.合成生物学 合成生物学とはトランスクリプション・ファクター

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Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
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関連する実験動画

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In vivo Application of the REMOTE-control System for the Manipulation of Endogenous Gene Expression
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Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
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科学分野:

  • 分子生物学は分子生物学である.
  • ゲノミクスゲノミクスとは
  • バイオフィジックス 生物物理学

背景:

  • 本質的に乱れた領域 (IDR) は,転写因子 (TF) を含む多くのタンパク質の機能に不可欠です.
  • TFs内のIDRが特定のゲノム認識を媒介するメカニズムは,まだ完全に理解されていません.
  • IDR配列の決定因子を理解することは,TF-ゲノム相互作用を解読する鍵です.

研究 の 目的:

  • 固有の無秩序領域 (IDR) 配列が特定のゲノム認識をどのようにコードするかを支配する原則を定義する.
  • 転写因子結合を誘導するIDR内の水害性アミノ酸分布の役割を調査する.
  • 選択的ゲノムターゲティングを行うことができる新しいIDRを設計する.

主な方法:

  • 185の新しい内在的に乱れた領域 (IDR) の設計と合成.
  • 排水性アミノ酸の分散の系統的変化と構造物の性質の乱れ.
  • 合成IDRの標的特異性を評価するために,芽生える酵母における全ゲノム結合分析.

主要な成果:

  • デノボ設計のIDRは,ネイティブTFとシーケンスの類似性がなく,ゲノム結合を誘導する活性を示した.
  • 合成IDRの結合特異性は,水害性拡散と障害の支架を変更することによって調整可能でした.
  • 何百もの酵母プロモーターにわたって,配列指向の結合偏好の連続性が観察されました.

結論:

  • IDR配列は,ネイティブ因子に対する配列ホモロジーから独立して,特定のゲノム認識原理をコードすることができます.
  • 水性性構造体内の水害性残留物の空間的分布は,IDR媒介結合特異性の重要な決定因子である.
  • これらの発見は,選択的なDNA結合タンパク質を理解し,設計するための基礎を提供します.