Related Experiment Video
Updated: Jun 16, 2026
Examination of Proteins Bound to Nascent DNA in Mammalian Cells Using BrdU-ChIP-Slot-Western Technique
Published on: January 14, 2016
Increased interaction between DJ-1 and the Mi-2/ nucleosome remodelling and deacetylase complex during cellular
Jill A Opsahl1, Linda V Hjørnevik, Vibeke H Bull
1Proteomic Unit (PROBE), Department of Biomedicine, University of Bergen, Bergen, Norway.
Abstract:
DJ-1 was originally identified to be an oncogenic product, but has later been shown to be highly multifunctional. DJ-1 plays a role in oxidative stress response and transcriptional regulation, and loss of its function leads to an early onset of Parkinsonism. To further understand the mechanisms behind DJ-1's role in cell survival and death, we investigated alternations in endogenous DJ-1 protein-protein interaction in apoptotic cells exposed to the phosphatase inhibitor okadaic acid. By combining cellular stable isotopic labelling of amino acids in cell culture, sub-cellular fractionation, co-immunoprecipitation, and MS, we identified a novel group of DJ-1 interaction partners that increased their association to DJ-1 in okadaic acid-exposed cells. These proteins were integral components of the Mi-2/nucleosome remodelling and deacetylase (NuRD) complex. Knockdown of DJ-1 and MTA2, a core component of the NuRD complex, had a similar and pro-apoptotic effect on the transcriptional- and p53-dependent cell death induced by daunorubicin. On the other hand, MTA2 knockdown had no significant effect on the progression of p53-independent okadaic acid-induced apoptosis. Our data suggest that the increased DJ-1/NuRD interaction is a general anti-stress response regulated by okadaic acid-induced modifications of DJ-1. The observed interaction between DJ-1 and the NuRD complex may give new clues to how DJ-1 can protect cells from p53-dependent cell death.
Insights
DJ-1 protein interacts with the NuRD complex during cellular stress, suggesting a role in protecting cells from p53-dependent death. This interaction is a key anti-stress response.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- DJ-1 is a multifunctional protein involved in oxidative stress response and transcriptional regulation.
- Loss of DJ-1 function is linked to Parkinsonism.
- The role of DJ-1 in cell survival and death mechanisms requires further elucidation.
Purpose of the Study:
- To investigate alterations in DJ-1 protein-protein interactions during apoptosis.
- To identify novel DJ-1 interaction partners in cells treated with okadaic acid.
- To understand DJ-1's role in cell death pathways, particularly p53-dependent apoptosis.
Main Methods:
- Cellular stable isotopic labeling of amino acids in cell culture.
- Sub-cellular fractionation and co-immunoprecipitation.
- Mass spectrometry (MS) to identify protein interactions.
Main Results:
- A novel group of DJ-1 interaction partners, integral to the Mi-2/nucleosome remodelling and deacetylase (NuRD) complex, was identified.
- Increased association of DJ-1 with the NuRD complex was observed in okadaic acid-exposed cells.
- Knockdown of DJ-1 and MTA2 (a NuRD component) exhibited similar pro-apoptotic effects on p53-dependent cell death.
Conclusions:
- The increased DJ-1/NuRD interaction represents a general anti-stress response mediated by okadaic acid-induced DJ-1 modifications.
- This interaction may provide new insights into DJ-1's protective function against p53-dependent cell death.
- DJ-1's interaction with the NuRD complex is a significant finding for understanding cell survival mechanisms.
Related Concept Videos
02:54Nucleosome Remodeling
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
01:32Chromatin Modification in iPS Cells
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
02:05Duplication of Chromatin Structure
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...
02:25Spreading of Chromatin Modifications
Writers
The writer is an enzyme that can...
02:32Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:32Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...