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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

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Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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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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Human Ccr4-Not complexes contain variable deadenylase subunits.

Nga-Chi Lau1, Annemieke Kolkman, Frederik M A van Schaik

  • 1Department of Physiological Chemistry, University Medical Center Utrecht, Utrecht, The Netherlands.

The Biochemical Journal
|June 30, 2009
PubMed
Summary
This summary is machine-generated.

The human Ccr4-Not complex, crucial for mRNA regulation, exists in at least four variants. These complexes contain core proteins and distinct deadenylase subunits, suggesting diverse cellular roles.

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Area of Science:

  • Molecular Biology
  • Proteomics
  • Gene Regulation

Background:

  • The Ccr4-Not complex is a conserved cellular machinery regulating mRNA synthesis and decay.
  • While the yeast Ccr4-Not complex is well-characterized, the human counterpart's composition and variations are less understood.
  • Human cells possess multiple subunits with mRNA deadenylase activity, hinting at complexity within the Ccr4-Not machinery.

Purpose of the Study:

  • To comprehensively investigate the composition and heterogeneity of the human Ccr4-Not complex.
  • To identify distinct variants of the human Ccr4-Not complex and their associated subunits.
  • To explore the functional implications of Ccr4-Not complex heterogeneity in cellular processes.

Main Methods:

  • Utilized stable cell lines expressing tagged CNOT proteins for proteomic analysis.
  • Employed in-depth proteomic approaches to identify complex components.
  • Analyzed associated proteins to infer functional roles of Ccr4-Not complexes.

Main Results:

  • Identified at least four distinct variants of the human Ccr4-Not complex.
  • Found seven stable core proteins common to these variants.
  • Discovered mutually exclusive mRNA deadenylase subunits associated with different complex variants.
  • Observed human CNOT4 forming a separate ~200 kDa complex.
  • Associated proteins suggest roles in RNA splicing, transport, and localization.

Conclusions:

  • Human Ccr4-Not complexes exhibit significant compositional heterogeneity driven by variations in deadenylase subunits.
  • This heterogeneity likely underlies the multi-functional roles of Ccr4-Not complexes in diverse cellular processes.
  • The findings provide a deeper understanding of gene regulation mechanisms in human cells.