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Related Concept Videos

Ribozymes02:47

Ribozymes

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...
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Catalysis02:50

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Protein Complex Assembly02:41

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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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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Preparation of Silica Nanoparticles Through Microwave-assisted Acid-catalysis
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Polyanion-Assisted Ribozyme Catalysis Inside Complex Coacervates.

Raghav R Poudyal, Christine D Keating, Philip C Bevilacqua

    ACS Chemical Biology
    |June 12, 2019
    PubMed
    Summary
    This summary is machine-generated.

    Polyanions boost ribozyme reactions within complex coacervates, acting as prebiotic compartments. By preventing RNA from binding to polycations, these polyanions enhance ribozyme catalysis over 12-fold.

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    Area of Science:

    • Biochemistry
    • Astrobiology
    • Origin of Life Studies

    Background:

    • Complex coacervates, formed by oppositely charged polyelectrolytes, are proposed as prebiotic nonmembranous compartments (NMCs).
    • These NMCs can sequester RNA and enhance ribozyme activity, supporting the RNA World Hypothesis.
    • The role of polyanionic components in modulating ribozyme catalysis within NMCs is not well understood.

    Purpose of the Study:

    • To investigate the mechanism by which polyanionic components influence ribozyme catalysis in complex coacervates.
    • To determine if diverse polyanions can enhance ribozyme activity in NMCs.

    Main Methods:

    • Formation of complex coacervates using various polyanions and polycations.
    • Assay of ribozyme activity (hammerhead and hairpin ribozymes) in the presence of coacervates and different polyanions.
    • Analysis of RNA-polycation interactions.

    Main Results:

    • Diverse polyanions, including polycarboxylates and polysulfates, significantly enhance ribozyme catalysis in complex coacervates, with increases exceeding 12-fold.
    • Polyanions act by competing with RNA for binding to polycationic coacervate components, thereby reducing unproductive interactions.
    • This enhancement mechanism was observed for both hammerhead and hairpin ribozymes, indicating generality.

    Conclusions:

    • Polyanions play a crucial role in enhancing ribozyme catalysis within complex coacervates.
    • The findings suggest a general mechanism for polyanion-mediated enhancement of RNA catalysis relevant to prebiotic chemistry.
    • These results highlight potential roles for polyanions in both the origin of life and extant biological systems.