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 Experiment Videos

RecA protein self-assembly. Multiple discrete aggregation states.

S L Brenner1, A Zlotnick, J D Griffith

  • 1Central Research and Development Department, E. I. du Pont de Nemours and Co., Inc., Wilmington, DE 19880-0328.

Journal of Molecular Biology
|December 20, 1988
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

The effects of children on divorce and re-marriage: a multivariate analysis of life table probabilities.

Population studies·2011
Same author

Innocuous Transportation of the Dead.

Public health papers and reports·2009
Same author

Validation of NMR relaxation exchange time measurements in porous media.

The Journal of chemical physics·2007
Same author

Structural features of the single-stranded DNA-binding protein of Epstein-Barr virus.

Journal of structural biology·2007
Same author

Evolving micro-structures in drying detergent pastes quantified using NMR.

Journal of colloid and interface science·2007
Same author

Experimental setup for low-energy laser-based angle resolved photoemission spectroscopy.

The Review of scientific instruments·2007
Same journal

UPF3A and UPF3B shape the transcriptome cooperatively yet oppose cell function.

Journal of molecular biology·2026
Same journal

Antibody-secreting cells integrate efficient NMD with non‑canonical UPR signaling to maintain proteostasis and support massive immunoglobulin synthesis.

Journal of molecular biology·2026
Same journal

Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

Journal of molecular biology·2026
Same journal

UPF1 at Work: Structural and Mechanistic Insights Into a Master Regulator of Nonsense-Mediated mRNA Decay.

Journal of molecular biology·2026
Same journal

Structural basis for the pro-amyloidogenic action and ligand binding of a novel W72R variant of human apolipoprotein A-I.

Journal of molecular biology·2026
Same journal

Cryo-EM Structure of the C. Elegans Septin Tetramer Reveals a Revised Architecture and Conserved Positional Orthology.

Journal of molecular biology·2026
See all related articles

RecA protein self-assembles into various structures based on concentration and ionic conditions. These RecA protein structures, including rods and rings, are crucial for its function in DNA repair.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • RecA protein is essential for DNA repair and recombination.
  • Understanding RecA protein aggregation is key to elucidating its mechanism of action.

Purpose of the Study:

  • To investigate the aggregation states of purified RecA protein in solution.
  • To determine how environmental factors influence RecA protein quaternary structures.

Main Methods:

  • Light scattering
  • Sedimentation analysis
  • Electron microscopy

Main Results:

  • RecA protein self-assembles into discrete quaternary structures (4 nm, 12 nm particles, rods, bundles).

Related Experiment Videos

  • Protein concentration, ionic environment, and nucleotide cofactors dictate aggregation states.
  • Monovalent salts shift oligomeric distribution; MgCl2 promotes rod and bundle formation.

    • Conclusions:

    • RecA protein aggregation is concentration-dependent and influenced by ionic conditions.
    • Specific RecA protein structures (rods, 12 nm particles) are prevalent under in vitro strand exchange conditions.