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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...
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,...
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.

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Related Experiment Video

Updated: May 15, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
08:07

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

RVBs are required for assembling a functional TIP60 complex.

Sudhakar Jha1, Ashish Gupta, Ashraf Dar

  • 1Department of Biochemistry and Molecular Genetics, University of Virginia, School of Medicine, Charlottesville, Virginia, USA.

Molecular and Cellular Biology
|January 9, 2013
PubMed
Summary
This summary is machine-generated.

RuvBL1/RuvBL2 (RVB) proteins act as molecular adaptors in the TIP60 complex, ensuring its stability and function. They displace p400 to enable TIP60 activity and maintain complex heat stability, independent of their ATPase function.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Last Updated: May 15, 2026

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

  • Molecular biology
  • Chromatin remodeling
  • Protein complex assembly

Background:

  • RuvBL1/RuvBL2 (RVB) proteins are AAA+ ATPases found in various cellular complexes.
  • Their precise molecular roles within these complexes remain unclear.
  • The TIP60 complex, a tumor suppressor, utilizes RVB proteins for its chromatin-remodeling functions.

Purpose of the Study:

  • To elucidate the specific molecular functions of RVB proteins within the TIP60 complex.
  • To understand how RVBs contribute to the catalytic activity and stability of TIP60.com.
  • To investigate the redundancy and ATPase-independent roles of RVB1 and RVB2.

Main Methods:

  • Investigated the interaction between RVBs, TIP60, and p400 within the TIP60 complex.
  • Assessed the impact of RVBs on TIP60's lysine acetyltransferase activity.
  • Examined the heat stability of the TIP60 complex under different conditions.
  • Evaluated the necessity of RVB ATPase activity for their functions.

Main Results:

  • RVBs competitively displace the SNF2 domain of p400, relieving p400-mediated repression of TIP60's catalytic activity.
  • RVBs are essential for the heat stability of the TIP60 complex via a p400-independent mechanism.
  • RVB1 and RVB2 exhibit functional redundancy and do not require their ATPase activity for these roles.
  • RVB proteins function as adaptable molecular scaffolds within the TIP60 complex.

Conclusions:

  • RVB proteins are crucial for the assembly, stability, and optimal function of the TIP60 complex.
  • They act as versatile molecular adaptors, substituting for each other to regulate TIP60 activity and complex integrity.
  • The findings highlight a novel mechanism for regulating chromatin-remodeling complex function through protein-protein interactions and scaffolding.