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

Evolutionally conserved intermediates between ubiquitin and NEDD8.

Ryo Kitahara1, Yoshiki Yamaguchi, Eri Sakata

  • 1RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-chou, Sayo-gun, Hyogo, 679-5148, Japan.

Journal of Molecular Biology
|September 19, 2006
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

Blm10/PA200-Activated 20S Proteasomes Promote α-Synuclein Degradation and Bypass Proteasome Inhibition in Parkinson's Disease Models.

Aging cell·2026
Same author

The vacuolar tauopathy-associated mutation D395G confers redox sensitivity to p97/VCP.

bioRxiv : the preprint server for biology·2026
Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026
Same author

Structures of the 26<i>S</i> proteasome in complex with the Hsp70 co-chaperone Bag1 reveal a mechanism for direct substrate transfer.

Science advances·2026
Same author

Use of High Pressure NMR Spectroscopy to Rapidly Identify Proteins with Internal Ligand-Binding Voids.

bioRxiv : the preprint server for biology·2025
Same author

Inhibition of 26S proteasome activity by α-synuclein is mediated by the proteasomal chaperone Rpn14/PAAF1.

Aging cell·2024
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

Ubiquitin and NEDD8 proteins share similar structures but differ in function. Differences in their thermodynamic stability and disordered states explain their distinct physiological roles.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • Proteins with similar topologies can have divergent amino acid sequences.
  • The ubiquitin superfold is a common structural motif found in proteins with conserved topologies but poor sequence conservation.

Purpose of the Study:

  • To investigate novel similarities and differences between ubiquitin and NEDD8 proteins.
  • To understand how structural similarity relates to functional divergence.

Main Methods:

  • Variable pressure Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Analysis of conformational fluctuations and thermodynamic stability.

Main Results:

  • Ubiquitin and NEDD8 share 57% sequence identity, similar backbone topology, and functional strategies, despite different physiological functions.

Related Experiment Videos

  • Both proteins exhibit similar conformational fluctuations in enzyme-binding regions and possess a disordered conformer (I) in equilibrium with a folded conformer (N).
  • NEDD8 shows a significantly higher population of the disordered conformer (I) and a greater tendency for overall unfolding (U) compared to ubiquitin, indicating lower thermodynamic stability.
  • Conclusions:

    • Differences in the thermodynamic stabilities of disordered conformers and unfolding species are critical for the distinct physiological functions of structurally similar proteins like ubiquitin and NEDD8.
    • Protein structural similarity does not always equate to functional similarity, with dynamics and stability playing key roles.