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RNA Editing02:23

RNA Editing

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RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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...
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Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

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In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps...
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Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Robust mammalian RNA localization elements are complex and multipartite.

bioRxiv : the preprint server for biology·2026
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ZBP1's Inability to Convert Unmodified RNAs to the Z-form Underlies a Balanced Mechanism of RNA Recognition with ADAR1.

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Zα and Zβ domains of ADAR1 and ZBP1 bind G-quadruplexes with nanomolar affinities, establishing Zβ as a G-quadruplex-specific domain.

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Related Experiment Video

Updated: Jun 13, 2025

Efficient PAM-Less Base Editing for Zebrafish Modeling of Human Genetic Disease with zSpRY-ABE8e
07:31

Efficient PAM-Less Base Editing for Zebrafish Modeling of Human Genetic Disease with zSpRY-ABE8e

Published on: February 17, 2023

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Z-Form Stabilization By The Zα Domain Of Adar1p150 Has Subtle Effects On A-To-I Editing.

Parker J Nichols, Kent A Riemondy, Jeffrey B Krall

    Biorxiv : the Preprint Server for Biology
    |June 12, 2025
    PubMed
    Summary
    This summary is machine-generated.

    The Zα domain of Adenosine Deaminase Acting on RNA 1 (ADAR1) has a minor role in A-to-I RNA editing. Phenotypes in Zα mutants may stem from altered interactions with Z-DNA-Binding Protein 1 (ZBP1), not RNA editing changes.

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    A Nonsequencing Approach for the Rapid Detection of RNA Editing
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    A Nonsequencing Approach for the Rapid Detection of RNA Editing

    Published on: April 21, 2022

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    Area of Science:

    • Molecular Biology
    • RNA Biology
    • Genetics

    Background:

    • Adenosine Deaminase Acting on RNA 1 (ADAR1) catalyzes A-to-I RNA editing.
    • The Zα domain of ADAR1 is implicated in stabilizing RNA structures, but its precise role in editing is debated.
    • Previous studies faced technical challenges in assessing Zα function due to variable ADAR1 expression and localization.

    Purpose of the Study:

    • To investigate the role of ADAR1's Zα domain in A-to-I RNA editing using a controlled cellular system.
    • To differentiate between editing-dependent and editing-independent functions of the Zα domain.

    Main Methods:

    • Generated stable cell lines expressing wild-type and Zα mutant ADAR1p150 using a Cre-lox system in ADAR1p150 knockout cells.
    • Performed total RNA sequencing to analyze A-to-I editing events.
    • Quantified editing clusters as a proxy for double-stranded RNA (dsRNA) substrates.
    • Assessed ADAR1p150 localization in cells.

    Main Results:

    • Zα mutations caused a slight decrease in overall A-to-I editing.
    • The observed reduction in editing correlated with ADAR1p150 mislocalization, not altered editing specificity.
    • No statistically significant differentially edited sites were found between wild-type and Zα mutant ADAR1p150.
    • ADAR1p150 mislocalization was a key factor in reduced editing efficiency.

    Conclusions:

    • The Zα domain's contribution to A-to-I RNA editing is minimal.
    • Observed phenotypes in Zα mutant models likely result from editing-independent inhibition of Z-DNA-Binding Protein 1 (ZBP1).
    • This study clarifies the functional role of the Zα domain in ADAR1-mediated RNA editing.