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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Electron Transport Chain: Complex I and II01:46

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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Protein Transport to the Stroma01:24

Protein Transport to the Stroma

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Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
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RNA Structure01:19

RNA Structure

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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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  1. Home
  2. Research Domains
  3. Biomedical And Clinical Sciences
  4. Neurosciences
  5. Cellular Nervous System
  6. Structure Of The Human Tip60 Complex.
  1. Home
  2. Research Domains
  3. Biomedical And Clinical Sciences
  4. Neurosciences
  5. Cellular Nervous System
  6. Structure Of The Human Tip60 Complex.

Related Experiment Video

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
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Structure of the human TIP60 complex.

Ke Chen1, Li Wang2, Zishuo Yu1

  • 1Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Shanghai Key Laboratory of Medical Epigenetics, Shanghai Medical College of Fudan University, Shanghai, 200032, China.

Nature Communications
|August 17, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

The human TIP60 complex

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Mammalian TIP60 is a crucial enzyme involved in transcription, DNA repair, and cell cycle control.
  • It possesses histone acetylation and histone dimer exchange activities.
  • Understanding its structure is key to deciphering its diverse cellular functions.

Purpose of the Study:

  • To determine the high-resolution cryo-electron microscopy structures of the human TIP60 complex.
  • To elucidate the molecular architecture and subunit organization of TIP60.
  • To provide insights into how TIP60 interacts with nucleosomes.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) at 3.2-Å resolution.
  • Structural refinement of the human TIP60 complex, including core and TRRAP modules.
  • Analysis of protein-protein interactions within the complex.
  • Main Results:

    • The EP400 protein serves as a central scaffold, integrating motor, ARP, and TRRAP modules.
    • Specific protein interactions define the assembly of the motor module (RUVBL1-RUVBL2 hexamer, EP400 ATPase, YL1) and the ARP module (ACTL6A-ACTB heterodimer, DMAP1, EPC1).
    • The ARP module shows stable association with the motor module but flexible tethering to the TRRAP module, with an unengaged nucleosome positioned between the core and TRRAP modules.

    Conclusions:

    • The study reveals the detailed molecular architecture of the human TIP60 complex.
    • The findings offer structural insights into the TIP60 complex's interaction with nucleosomes.
    • This work lays the foundation for understanding TIP60's role in various cellular processes.