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Related Concept Videos

Nucleotide Excision Repair01:38

Nucleotide Excision Repair

DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

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Related Experiment Video

Updated: Jun 11, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Oxidative stress induces mainly human centrin 2 polymerisation.

Emilie Brun1, Yves Blouquit, Patricia Duchambon

  • 1Laboratoire de Chimie Physique, CNRS UMR 8000, Université Paris-Sud 11, Bât. 350, Orsay Cedex, France.

International Journal of Radiation Biology
|July 1, 2010
PubMed
Summary

Oxidizing radicals cause human centrin 2 (Hscen 2) protein to polymerize, forming cross-links. This radiation-induced damage affects Hscen 2

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Area of Science:

  • Biochemistry
  • Protein chemistry
  • Radiation biology

Background:

  • Human centrin 2 (Hscen 2) is a key protein involved in cellular processes.
  • Understanding protein response to oxidative stress is crucial for cell biology.

Purpose of the Study:

  • To investigate the in vitro response of Hscen 2 to oxidizing radicals.
  • To evaluate the functional consequences of radical-induced Hscen 2 modifications.

Main Methods:

  • Hscen 2 was exposed to hydroxyl and azide radicals via radiolysis.
  • Products were analyzed using biochemical, spectroscopic, and mass spectrometry.
  • Complexation thermodynamics with C-XPC were quantified using isothermal titration calorimetry (ITC).

Main Results:

  • Hydroxyl and azide radicals induced Hscen 2 polymerization through intermolecular cross-links.
  • Cross-linking occurred at the sole tyrosine residue (Tyr 172).
  • Dimerization occurred at low radiation doses, reducing binding affinity to C-XPC.

Conclusions:

  • Hscen 2 is highly sensitive to ionizing radiation, exhibiting significant polymerization.
  • Oxidative radical-induced damage to Hscen 2 can impair its biological functions.
  • The findings highlight potential implications for cellular repair mechanisms.