AI Article Synopsis
- Deoxyinosine (dI) in DNA is a significant source of genetic mutations, potentially leading to cancer and other diseases, highlighting the need to understand dI-binding proteins.
- A proteomics approach was used to identify proteins that interact with dI in DNA, revealing that human mitochondrial heat shock protein 60 (HSPD1) binds to dI-bearing DNA.
- HSPD1 was shown to be involved in responding to sodium nitrite-induced DNA damage and regulating dI levels, suggesting its crucial role in mitochondrial DNA damage control.
Article Abstract
The generation of deoxyinosine (dI) in DNA is one of the most important sources of genetic mutations, which may lead to cancer and other human diseases. A further understanding of the biological consequences of dI necessitates the identification and functional characterizations of dI-binding proteins. Herein, we employed a mass spectrometry-based proteomics approach to detect the cellular proteins that may sense the presence of dI in DNA. Our results demonstrated that human mitochondrial heat shock protein 60 (HSPD1) can interact with dI-bearing DNA. We further demonstrated the involvement of HSPD1 in the sodium nitrite-induced DNA damage response and in the modulation of dI levels and in human cells. Together, these findings revealed HSPD1 as a novel dI-binding protein that may play an important role in the mitochondrial DNA damage control in human cells.
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| http://dx.doi.org/10.1021/acs.jproteome.2c00854 | DOI Listing |
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