Ribonucleoprotein Assembly
Ribonucleoprotein Assembly - Related Videos
07:46
CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.
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Cited by 7 •
2020
The goal of this protocol is to enable seamless CRISPR/Cas9 editing of the C. elegans genome using assembled ribonucleoprotein complexes and the dpy-10 co-CRISPR marker for screening. This protocol can be used to make a variety of genetic modifications in C. elegans including insertions, deletions, gene replacements and codon substitutions.
08:56
In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
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Cited by 10 •
2020
This protocol demonstrates use of the proximity ligation assay to probe for protein-protein interactions in situ in the C. elegans germline.
07:20
Generation of Knock-out Primary and Expanded Human NK Cells Using Cas9 Ribonucleoproteins
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Cited by 53 •
2018
Here, we present a protocol to genetically modify primary or expanded human natural killer (NK) cells using Cas9 Ribonucleoproteins (Cas9/RNPs). By using this protocol, we generated human NK cells deficient for transforming growth factor–b receptor 2 (TGFBR2) and hypoxanthine phosphoribosyltransferase 1 (HPRT1).
09:51
Enhanced Genome Editing with Cas9 Ribonucleoprotein in Diverse Cells and Organisms
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Cited by 45 •
2018
Utilizing a preassembled Cas9 ribonucleoprotein complex (RNP) is a powerful method for precise, efficient genome editing. Here, we highlight its utility across a broad range of cells and organisms, including primary human cells and both classic and emerging model organisms.
01:38
Remodeling of Viral Ribonucleoprotein Activity Through Recombinant Polymerase and Host Protein
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2026
Begin with influenza virus-derived viral ribonucleoprotein or vRNP complexes.The vRNP complex contains an RNA polymerase bound to the viral RNA genome, essential for viral RNA synthesis.Add increasing amounts of a recombinant viral polymerase, along with a recombinant host protein, to mimic host-mediated regulation of vRNP activity.Introduce capped RNA as a primer to initiate transcription.Add nucleotide and polymerase cofactors to promote vRNP activity, and RNase inhibitors to inactivate the...
FAQs
RNA-binding proteins can recognize particular RNA sequences or structural features, giving assembly a degree of molecular selectivity. RNA folding creates shapes that influence which proteins can bind and where they associate. These recognition events help organize the developing complex rather than producing random contacts, allowing the resulting ribonucleoprotein to support a defined cellular task.
Cooperative interactions allow one binding event to promote additional associations within the same complex. This coordination can stabilize the growing structure and help organize multiple RNA and protein components into a functional arrangement. Cooperative behavior is therefore relevant to understanding how ribonucleoprotein complexes achieve ordered assembly and how their formation may be controlled.
Assembly factors help organize ribonucleoprotein components and promote maturation after initial RNA-protein recognition. Their involvement distinguishes an incompletely assembled complex from one that has reached a functional state. Examining these factors helps explain how large RNA-protein machines become properly organized and how cells control the progression from early interactions to mature complexes.
The underlying principles of RNA recognition, protein association, folding, and maturation can apply to several complexes, but their biological roles differ. Ribosomes support translation, spliceosomes participate in RNA processing, and telomerase represents another major RNA-protein machine. Comparing them shows how related assembly principles generate complexes specialized for distinct aspects of gene expression and chromosome maintenance.
A useful investigation considers the RNA sequence, its folded structural features, the proteins that recognize it, and the interactions that organize the complex. Researchers can also examine assembly factors and maturation because these features connect initial binding with functional organization. Together, these considerations provide a framework for interpreting how a ribonucleoprotein complex forms and becomes active.
Studies can clarify how RNA-processing, transport, translation, and regulatory complexes are built and controlled. They also connect molecular interactions with RNA quality control and with disorders associated with defective RNA or protein interactions. This makes the topic relevant both to basic studies of gene expression and to investigations of biological consequences that arise when complex formation is disrupted.