Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Cytoskeletal Proteins in Bacteria

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...

Fimbriae, Pili, and Axial Filaments

Fimbriae, Pili, and Axial Filaments

Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...

Protein Complex Assembly

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...

Coordination of Gene Expression Processes in Bacteria

Coordination of Gene Expression Processes in Bacteria

The DNA replication, transcription, and translation processes are intricately coupled in bacteria, allowing efficient gene expression and rapid protein synthesis. While this physical and functional coordination is advantageous, it introduces challenges that bacteria overcome through specific regulatory mechanisms.Coupling of Replication, Transcription, and TranslationThe coupling of replication, transcription, and translation is a hallmark of bacterial gene expression. As the replisome unwinds...

Protein Complexes with Interchangeable Parts

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 Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

You might also read

Related Articles

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

Sort by

Same author

Characterization of a mechanistic connection between persulfide transfer and ATP hydrolysis in the SufBC2D scaffold of the Suf Fe-S cluster assembly pathway.

Metallomics : integrated biometal science·2025

Same author

Escherichia coli monothiol glutaredoxin GrxD replenishes Fe-S clusters to the essential ErpA A-type carrier under low iron stress.

The Journal of biological chemistry·2024

Same author

Facial amphiphilic naphthoic acid-derived antimicrobial polymers against multi-drug resistant gram-negative bacteria and biofilms.

Biomaterials·2023

Same author

Ni-NTA Affinity Chromatography to Characterize Protein-Protein Interactions During Fe-S Cluster Biogenesis.

Methods in molecular biology (Clifton, N.J.)·2021

Same author

Fe-S cluster biogenesis by the bacterial Suf pathway.

Biochimica et biophysica acta. Molecular cell research·2020

Same author

Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues.

The Journal of biological chemistry·2019

Search research articles

Related Experiment Video

Updated: Jul 6, 2026

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

Published on: November 12, 2012

Fe-S cluster assembly pathways in bacteria.

Carla Ayala-Castro¹, Avneesh Saini, F Wayne Outten

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

Microbiology and Molecular Biology Reviews : MMBR

|March 7, 2008

Summary

Iron-sulfur (Fe-S) clusters are vital for cellular processes. This review summarizes recent advances in understanding Fe-S cluster assembly pathways and highlights new research directions in this complex field.

More Related Videos

FtsZ Polymerization Assays: Simple Protocols and Considerations

FtsZ Polymerization Assays: Simple Protocols and Considerations

Published on: November 16, 2013

Super-resolution Imaging of the Bacterial Division Machinery

Super-resolution Imaging of the Bacterial Division Machinery

Published on: January 21, 2013

Related Experiment Videos

Last Updated: Jul 6, 2026

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

Published on: November 12, 2012

FtsZ Polymerization Assays: Simple Protocols and Considerations

FtsZ Polymerization Assays: Simple Protocols and Considerations

Published on: November 16, 2013

Super-resolution Imaging of the Bacterial Division Machinery

Super-resolution Imaging of the Bacterial Division Machinery

Published on: January 21, 2013

Area of Science:

Biochemistry
Molecular Biology
Microbiology

Background:

Iron-sulfur (Fe-S) clusters are essential cofactors for numerous critical cellular processes, including respiration, photosynthesis, and nitrogen fixation.
The assembly of Fe-S clusters is a tightly regulated process to prevent cellular toxicity from free iron and sulfide.
Bacteria possess diverse Fe-S cluster assembly pathways, catering to basal, stress-responsive, and enzyme-specific needs.

Purpose of the Study:

To provide a comprehensive summary of recent advancements in the field of Fe-S cluster assembly.
To highlight emerging research areas and unanswered mechanistic questions in Fe-S cluster biogenesis.
To integrate newly identified factors into existing models of Fe-S cluster assembly and repair.

Main Methods:

Literature review of recent biochemical and genetic studies.
Analysis of newly identified proteins involved in Fe-S cluster metabolism.
Synthesis of current knowledge to identify gaps and future research directions.

Main Results:

Recent studies have identified novel factors and pathways contributing to Fe-S cluster assembly and repair.
The complexity of Fe-S cluster biogenesis models is expanding with new discoveries.
Biochemical and genetic characterization continues to refine our understanding of in vivo Fe-S cluster assembly.

Conclusions:

Significant progress has been made in understanding Fe-S cluster assembly, yet mechanistic details remain elusive.
The identification of new factors underscores the intricate nature of Fe-S cluster homeostasis.
Future research should focus on integrating new findings to develop more complete models of Fe-S cluster assembly and repair.