Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...

You might also read

Related Articles

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

Sort by
Same author

Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.

Chemical science·2026
Same author

Harmonizing Peak Matching Between Multidimensional NMR Spectra.

bioRxiv : the preprint server for biology·2026
Same author

Resolving heterogeneity of targeted lipid nanoparticles through solution-based biophysical analyses.

bioRxiv : the preprint server for biology·2026
Same author

Software for small-angle neutron scattering contrast variation experiment planning and data analysis.

Journal of applied crystallography·2026
Same author

Structures of nucleotide-bound Redondovirus Rep protein link conformation and function.

PLoS pathogens·2026
Same author

Author Correction: Elucidating lipid nanoparticle properties and structure through biophysical analyses.

Nature biotechnology·2026

Related Experiment Video

Updated: May 22, 2026

Using In Vitro and In-cell SHAPE to Investigate Small Molecule Induced Pre-mRNA Structural Changes
11:58

Using In Vitro and In-cell SHAPE to Investigate Small Molecule Induced Pre-mRNA Structural Changes

Published on: January 30, 2019

Solution structure of the core SMN-Gemin2 complex.

Kathryn L Sarachan1, Kathleen G Valentine, Kushol Gupta

  • 1Graduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.

The Biochemical Journal
|May 22, 2012
PubMed
Summary
This summary is machine-generated.

The survival of motor neuron (SMN) complex is crucial for assembling spliceosomal small nuclear ribonucleoproteins (snRNPs). This study reveals the structure of Gemin2 bound to SMN, uncovering new insights into snRNP assembly and spinal muscular atrophy.

More Related Videos

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
07:59

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination

Published on: August 17, 2022

Related Experiment Videos

Last Updated: May 22, 2026

Using In Vitro and In-cell SHAPE to Investigate Small Molecule Induced Pre-mRNA Structural Changes
11:58

Using In Vitro and In-cell SHAPE to Investigate Small Molecule Induced Pre-mRNA Structural Changes

Published on: January 30, 2019

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
07:59

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination

Published on: August 17, 2022

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • The survival of motor neuron (SMN) complex is essential for the biogenesis of spliceosomal small nuclear ribonucleoproteins (snRNPs).
  • SMN protein deficiency is linked to spinal muscular atrophy (SMA), a severe neurodegenerative disease.
  • Gemin2 is a key component of the SMN complex involved in snRNP assembly.

Purpose of the Study:

  • To determine the solution structure of the Gemin2-Gemin2-binding domain of SMN complex using NMR spectroscopy.
  • To elucidate the structural basis of Gemin2 binding to SMN.
  • To investigate the functional significance of conserved SMN residues in snRNP assembly.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the solution structure of the SMN-Gemin2 complex.
  • Structural analysis focused on the interaction interface between Gemin2 and the SMN protein.
  • Mutational analysis of conserved SMN residues was performed.

Main Results:

  • The solution structure of Gemin2 bound to the Gemin2-binding domain of SMN was determined.
  • The study details how Gemin2 binds to SMN and identifies conserved SMN residues involved.
  • Surprisingly, several conserved SMN residues, including those mutated in SMA patients, are not essential for Gemin2 binding but form a distinct functional surface.

Conclusions:

  • The determined SMN-Gemin2 structure provides a molecular basis for Gemin2 stabilization by SMN.
  • The findings reveal a conserved surface on SMN/Gemin2 potentially crucial for snRNP assembly.
  • This structural framework facilitates future research into snRNP biogenesis and Gemin2 functions beyond snRNP assembly.