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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...
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,...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...

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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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Published on: January 11, 2017

The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer.

Harsimranjit K Chahal1, Yuyuan Dai, Avneesh Saini

  • 1Department of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, South Carolina 29208, USA.

Biochemistry
|October 9, 2009
PubMed
Summary

Iron-sulfur (Fe-S) clusters are vital for cellular processes. This study reveals the SufBCD complex acts as a scaffold for Fe-S cluster assembly in E. coli, transferring them to the SufA shuttle protein.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Iron-sulfur (Fe-S) clusters are essential cofactors in numerous biological pathways, including nitrogen fixation and respiration.
  • In vivo Fe-S cluster assembly requires complex, multiprotein biosynthetic pathways due to the toxicity of iron and sulfide.
  • The SufABCDSE pathway in Escherichia coli is a stress-responsive system for Fe-S cluster assembly under conditions of iron starvation and oxidative stress.

Purpose of the Study:

  • To elucidate the specific roles of the SufBCD complex and SufA protein in the Suf Fe-S cluster biosynthesis pathway.
  • To investigate the mechanism of nascent Fe-S cluster formation and transfer within the Suf pathway.

Main Methods:

  • Protein-protein interaction assays were employed to study complex formation.
  • In vitro Fe-S cluster assembly assays were conducted to analyze the biochemical processes.
  • Characterization of the SufABCDSE pathway in Escherichia coli.

Main Results:

  • SufA was shown to interact with the SufBCD complex.
  • Fe-S clusters are assembled de novo on the SufBCD complex.
  • SufA accepts Fe-S clusters from the SufBCD complex, functioning as an Fe-S shuttle.

Conclusions:

  • The SufBCD complex serves as a novel scaffold for the assembly of nascent Fe-S clusters.
  • The SufBCD complex transfers newly formed Fe-S clusters to the SufA protein for subsequent delivery.
  • This study provides the first biochemical evidence for the scaffold function of SufBCD in Fe-S cluster biosynthesis.