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Related Concept Videos

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Nuclear reprogramming is the process of switching gene expression of one cell type to that of another cell type, usually from a differentiated cell state to an undifferentiated cell state. Differentiation occurs during processes such as development and morphogenesis, tissue regeneration, and malignancy. Cells can also be artificially induced to reprogram their gene expression by techniques such as nuclear transfer, induced pluripotency, and cell fusion. Such techniques have many applications in...
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Nuclear reprogramming is a process of transforming one cell type into an unrelated cell type by epigenetic changes that alter the cell’s original gene expression pattern. Such epigenetic changes force cells to express a different set of genes, which play a significant role in inducing transformation into other cell types. Nuclear reprogramming offers applications in reproductive cloning for livestock propagation and regenerative medicine — developing patient-specific cells for...
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Reprogramming alters the gene expression in somatic cells, transforming them into induced pluripotent stem (iPS) cells over several generations. Scientists can reprogram cells by introducing genes for four transcription factors—Oct4, Sox2, Klf4, and c-Myc (OSKM) by viral or non-viral methods. These factors are also known as Yamanaka factors after Shinya Yamanaka, who first generated iPS cells using mouse skin cells. Yamanaka was awarded the Nobel Prize in Physiology or Medicine in 2012...
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Stem cells are undifferentiated cells that divide and produce different types of cells. Ordinarily, cells that have differentiated into a specific cell type are post-mitotic—that is, they no longer divide. However, scientists have found a way to reprogram these mature cells so that they “de-differentiate” and return to an unspecialized, proliferative state. These cells are also pluripotent like embryonic stem cells—able to produce all cell types—and are therefore...
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Reprogramming a Deubiquitinase into a Transamidase.

Lin Hui Chang, Eric R Strieter

    ACS Chemical Biology
    |August 24, 2018
    PubMed
    Summary

    Researchers evolved a deubiquitinase to create self-ubiquitinated proteins, revealing how chain anchoring affects enzyme activity and ubiquitin signaling.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Ubiquitin Signaling

    Background:

    • Ubiquitin conjugates are crucial for understanding ubiquitin signaling.
    • Synthesizing ubiquitinated proteins with native isopeptide bonds is challenging.
    • The impact of anchored ubiquitin chains on deubiquitinase and ubiquitin-binding protein activity is poorly understood.

    Purpose of the Study:

    • To evolve a deubiquitinase capable of site-specific autoubiquitination.
    • To investigate the biochemical consequences of anchored ubiquitin chains on deubiquitinase activity.

    Main Methods:

    • Protein engineering and yeast display screening were used to evolve the deubiquitinase.
    • Site-specific autoubiquitination was achieved through mutagenesis.
    • The transamidation to hydrolysis ratio was measured to assess enzyme activity.

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    Main Results:

    • A variant of yeast ubiquitin C-terminal hydrolase Yuh1 showed a 28-fold improvement in transamidation to hydrolysis ratio.
    • This variant enabled robust autoubiquitination, forming an isopeptide bond.
    • Certain deubiquitinases exhibited extreme sensitivity to ubiquitin chain anchoring.

    Conclusions:

    • The evolved Yuh1 variant facilitates the study of anchored ubiquitin chains.
    • Ubiquitin chain anchoring significantly impacts deubiquitinase activity.
    • Investigating deubiquitinases with both anchored and unanchored chains is essential.