Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Restarting Stalled Replication Forks

Restarting Stalled Replication Forks

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, a...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

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...

ATP Synthase: Structure

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...

Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Molecular basis of allosteric regulation and pharmaceutical targeting of protein kinase Cβ.

Nature communications·2026

Same author

Topobexin targets the Topoisomerase II ATPase domain for beta isoform-selective inhibition and anthracycline cardioprotection.

Nature communications·2025

Same author

Recombinant Topoisomerase 2 Production Using Cultured Human Cell Lines.

Methods in molecular biology (Clifton, N.J.)·2025

Same author

The viral serpin SPI-1 directly inhibits the host cell serine protease FAM111A.

The Journal of biological chemistry·2025

Same author

Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay.

Journal of visualized experiments : JoVE·2024

Same author

Monocyte response to SARS-CoV-2 protein ORF8 is associated with severe COVID-19 infection in patients with chronic lymphocytic leukemia.

Haematologica·2024

Same journal

Optimized tRNA structure-seq reveals robust tRNA secondary structures in <i>S. cerevisiae</i> under mild stress conditions.

RNA (New York, N.Y.)·2026

Same journal

SERIPH: A Two-Step Extraction Protocol for Selective Enrichment of Semi-Extractable RNAs.

RNA (New York, N.Y.)·2026

Same journal

Reduced Sensitivity to RNA Structural Differences Distinguishes Eukaryotic Pus4 from Bacterial TruB.

RNA (New York, N.Y.)·2026

Same journal

Puf3 contributes to changes in mRNA solubility, translation elongation dynamics at rare arginine codons and loss of protein homeostasis in cells lacking Not4.

RNA (New York, N.Y.)·2026

Same journal

RBM38 Regulates HORMAD1 Splicing to Enhances MEK Inhibitor Sensitivity in Breast Cancer.

RNA (New York, N.Y.)·2026

Same journal

EF-P Inhibits Ribosomal α-Hydroxy Acid Incorporation: Strategic tRNA Body Selection for Co-incorporating α-Hydroxy Acids and Nonproteinogenic Amino Acids into Depsipeptides.

RNA (New York, N.Y.)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 6, 2026

Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System

Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System

Published on: February 9, 2017

Structural model of the p14/SF3b155 · branch duplex complex.

Matthew J Schellenberg¹, Erin L Dul, Andrew M MacMillan

¹Department of Biochemistry, School of Molecular and Systems Medicine, University of Alberta, Edmonton, Alberta, Canada.

RNA (New York, N.Y.)

|November 11, 2010

Summary

This summary is machine-generated.

Human p14 protein binds pre-mRNA early in spliceosome assembly. This interaction, crucial for splicing, involves specific recognition of the branch adenosine, suggesting it must be disrupted for the splicing reaction to proceed.

More Related Videos

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Published on: April 26, 2017

Analyzing and Building Nucleic Acid Structures with 3DNA

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Related Experiment Videos

Last Updated: Jun 6, 2026

Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System

Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System

Published on: February 9, 2017

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Published on: April 26, 2017

Analyzing and Building Nucleic Acid Structures with 3DNA

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Area of Science:

Molecular Biology
Structural Biology
RNA Processing

Background:

The spliceosome is a large molecular machine responsible for pre-mRNA splicing.
Human p14 (SF3b14) is a key component of the U2 small nuclear ribonucleoprotein (snRNP).
p14 interacts with the pre-mRNA branch adenosine during early spliceosome assembly.

Purpose of the Study:

To elucidate the structural basis of the interaction between human p14 and the pre-mRNA branch region.
To understand the role of this interaction in spliceosome assembly and function.

Main Methods:

X-ray crystallography of a p14/SF3b155 peptide complex.
Biochemical analysis of disulfide cross-linked protein-RNA complexes.
Small-angle X-ray scattering (SAXS).

Main Results:

A structural model of the p14 · bulged duplex interaction was determined.
Specific recognition of the branch adenosine by a pocket on the p14/SF3b155 complex was revealed.
The orientation of the bulged duplex RNA bound to the protein surface was established, burying the branch nucleotide.

Conclusions:

The p14/SF3b155 complex specifically binds the pre-mRNA branch adenosine.
This intimate association suggests the interaction must be disrupted for the first step of splicing to occur.
The findings provide insights into the dynamic rearrangements within the spliceosome during assembly.