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Related Concept Videos

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...
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 Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Microtubule Formation01:23

Microtubule Formation

Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation of...
Assembly of Cytoskeletal Filaments01:18

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...

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The MultiBac Protein Complex Production Platform at the EMBL
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The role of MukE in assembling a functional MukBEF complex.

Melanie Gloyd1, Rodolfo Ghirlando, Alba Guarné

  • 1Department of Biochemistry and Biomedical Sciences, HSC-4N57A, McMaster University, Hamilton, ON, Canada L8S 4K1.

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|August 23, 2011
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The MukB-MukE-MukF complex is vital for bacterial chromosome management. New structural data reveals how MukE protein interactions regulate this complex, impacting DNA condensation and segregation in E. coli.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • The MukB-MukE-MukF complex in E. coli is crucial for chromosome condensation and segregation.
  • MukB, a structural maintenance of chromosomes (SMC) protein, requires MukE and MukF for function.
  • MukF acts as a bridge between MukB and MukE.

Purpose of the Study:

  • To elucidate the novel structure of the E. coli MukE-MukF complex.
  • To investigate the role of alternative dimerization interfaces and cross-linking interactions of MukE.
  • To understand how MukE-MukE and MukB-MukE interactions regulate higher-order bacterial condensin structures.

Main Methods:

  • X-ray crystallography to determine the structure of the MukE-MukF complex.
  • Site-directed mutagenesis to create MukE variants.
  • Functional assays using a mukE∷kan strain to assess temperature sensitivity restoration.

Main Results:

  • A novel structure of the E. coli MukE-MukF complex was determined, revealing an alternative MukE dimerization interface.
  • Additional cross-linking interactions between adjacent MukE-MukF complexes mediated by MukE were identified.
  • A MukE variant with mutations on a specific surface did not restore function in a mukE∷kan strain, indicating critical protein-protein interactions.

Conclusions:

  • The MukE dimerization interface overlaps with the MukB-binding region, suggesting a regulatory mechanism.
  • Competing MukB-MukE and MukE-MukE interactions likely control the formation of higher-order bacterial condensin structures.
  • The findings provide new insights into the structural dynamics and regulation of bacterial chromosome organization.