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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
siRNA - Small Interfering RNAs02:30

siRNA - Small Interfering RNAs

Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional level in some cases. siRNAs are important for protecting cells against viral infections and silencing transposable genetic elements.
In the cytoplasm, siRNA is processed from a double-stranded RNA, which comes from either endogenous DNA transcription or exogenous sources like a virus. This double-stranded RNA is then cleaved by the ATP-dependent...
Experimental RNAi02:15

Experimental RNAi

RNA interference (RNAi) is a cellular mechanism that inhibits gene expression by suppressing its transcription or activating the RNA degradation process. The mechanism was discovered by Andrew Fire and Craig Mello in 1998 in plants. Today, it is observed in almost all eukaryotes, including protozoa, flies, nematodes, insects, parasites, and mammals. This precise cellular mechanism of gene silencing has been developed into a technique that provides an efficient way to identify and determine the...
piRNA - Piwi-interacting RNAs02:57

piRNA - Piwi-interacting RNAs

PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while only 2000 genes have been found for miRNAs. piRNAs can act at the transcriptional and post-transcriptional levels and have a vital role in silencing transposable elements present in germ cells. They are also involved in epigenetic silencing and activation. Previously, they were thought to function only in germ cells but new evidence suggests...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
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Related Experiment Video

Updated: May 8, 2026

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
07:22

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

Activating silent argonautes.

Mary Anne Kidwell, Jennifer A Doudna

    Nature Structural & Molecular Biology
    |August 29, 2013
    PubMed
    Summary
    This summary is machine-generated.

    Chimeric Argonaute proteins reveal that distant mutations can activate catalytic activity, suggesting a new mechanism for RNA interference gene silencing. This finding hints at novel, structurally mediated regulation of Argonaute endonuclease function.

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    Optogenetic Random Mutagenesis Using Histone-miniSOG in C. elegans
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    Optogenetic Random Mutagenesis Using Histone-miniSOG in C. elegans

    Published on: November 14, 2016

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    Last Updated: May 8, 2026

    Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
    07:22

    Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

    Published on: May 23, 2020

    Optogenetic Random Mutagenesis Using Histone-miniSOG in C. elegans
    04:51

    Optogenetic Random Mutagenesis Using Histone-miniSOG in C. elegans

    Published on: November 14, 2016

    Area of Science:

    • Molecular Biology
    • Genetics
    • Biochemistry

    Background:

    • Argonaute (AGO) proteins are central to RNA interference (RNAi) mediated gene silencing.
    • While multiple AGO proteins are involved, only AGO2 possesses known endonuclease activity to cleave messenger RNAs (mRNAs).
    • The precise regulation of AGO endonuclease activity remains incompletely understood.

    Discussion:

    • This study investigates the catalytic activity of Argonaute proteins using chimeric constructs.
    • Mutations introduced distal to the canonical catalytic center were found to unmask or enhance endonuclease activity.
    • These findings suggest a regulatory mechanism where structural changes influence AGO protein function.

    Key Insights:

    • Chimeric Argonaute proteins demonstrate that mutations distant from the active site can confer or enhance mRNA cleavage ability.
    • This reveals an unexpected pathway for activating intrinsic catalytic function within Argonaute proteins.
    • The results point towards a model of structurally mediated regulation of AGO endonuclease activity.

    Outlook:

    • Further research can elucidate the precise structural rearrangements that lead to the unmasking of catalytic activity.
    • Understanding this mechanism could lead to novel therapeutic strategies targeting gene expression.
    • This work expands our knowledge of the diverse regulatory mechanisms governing RNA interference pathways.