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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
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Related Experiment Video

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In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces
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In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

Published on: March 19, 2010

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Catching global interactions in vivo.

Yi Qiu1,2, Suming Huang3,2,4

  • 1Department of Anatomy and Cell Biology, University of Florida College of Medicine, Gainesville, FL 32610 USA.

Cell & Bioscience
|October 13, 2017
PubMed
Summary
This summary is machine-generated.

Researchers developed bait protein-protein interaction-sequencing (bPPI-seq) to identify protein interactions. This method revealed histone variant H2A.Z

Keywords:
ChromatinH2A.ZH2A.Z interacting proteinsTranscriptional regulationbPPI-seq

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Area of Science:

  • Molecular Biology
  • Genomics
  • Biochemistry

Background:

  • Histone proteins and transcription factors (TFs) are crucial for gene transcription and multicellular organism development.
  • Existing methods for identifying TF interacting partners, like antibody-mediated isolation and mass spectrometry, require enhancement for comprehensive functional characterization in the post-human genome era.

Purpose of the Study:

  • To develop a sensitive and robust strategy for globally identifying and characterizing in vivo protein-protein interactions.
  • To establish a novel method for functional characterization of transcription factor activities during biological processes.

Main Methods:

  • Introduction of bait protein-protein interaction-sequencing (bPPI-seq), a novel strategy for global in vivo protein-protein interaction analysis.
  • Application of bPPI-seq as a proof-of-principle to identify interacting partners of histone variant H2A.Z.

Main Results:

  • Genome-wide interacting partners of histone variant H2A.Z were identified.
  • The identified interacting proteins of H2A.Z are predominantly involved in transcriptional regulation.
  • These interactions are distinct from those of canonical histone H2A, highlighting functional differences.

Conclusions:

  • The bPPI-seq method is a sensitive and robust approach for characterizing protein complexes.
  • bPPI-seq can be widely applied to globally map transcription factor interacting partners and their associated molecular networks.
  • This technique offers new insights into the functional roles of histone variants in transcriptional regulation.