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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

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 Parts01:57

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 Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

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Related Experiment Video

Updated: May 8, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Multi-subunit collaboration enables Smc5/6 to function as a composite SUMO E3 complex.

Xiaoyu Xue1,2,3, Jiayi Fan4, Shibai Li4

  • 1Department of Chemistry and Biochemistry, Texas State University, San Marcos, Texas, USA.

Research Square
|May 7, 2026
PubMed
Summary
This summary is machine-generated.

The Smc5/6 complex acts as a DNA- and ATP-stimulated SUMO E3 enzyme. Its subunits collaborate, using DNA binding and ATP, to enhance protein SUMOylation for genome regulation.

Keywords:
ATPaseDNA bindingSUMO E3Sgs1Smc5/6

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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

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Related Experiment Videos

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • SUMO E3 enzymes regulate protein SUMOylation, a key cellular process.
  • The Nse2 E3 enzyme is a crucial subunit of the Smc5/6 complex, involved in genome protection.

Purpose of the Study:

  • To investigate the SUMOylation mechanism of the Smc5/6 complex.
  • To elucidate the roles of non-SUMO E3 subunits in Smc5/6-mediated SUMOylation.

Main Methods:

  • In vitro SUMOylation assays using budding yeast Smc5/6.
  • Cellular SUMOylation assays.
  • Mutational analysis of Smc5/6 subunits.

Main Results:

  • DNA significantly enhances Smc5/6 E3 activity by increasing enzyme-substrate proximity.
  • Four non-SUMO E3 subunits contribute to DNA-mediated stimulation through DNA binding.
  • ATP binding by SMC subunits promotes SUMOylation by altering Smc5/6-DNA/chromatin interactions and inducing conformational changes.

Conclusions:

  • The Smc5/6 complex functions as a specialized, composite SUMO E3.
  • Inter-subunit collaboration, DNA binding, and ATP are critical for efficient Smc5/6 SUMOylation activity.
  • This mechanism is vital for effective genome regulation.