The DNA damage response (DDR) system plays an important role in maintaining genome stability and preventing related diseases. The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. Lysine crotonylation (Kcr) is a newly identified PTM occurring in both core histone and non-histone proteins in various organisms. This novel PTM is classified as a reversible acylation modification, which is regulated by a variety of acylases and deacylases and the intracellular crotonyl-CoA substrate concentration. Recent studies suggest that Kcr links cellular metabolism with gene regulation and is involved in numerous cellular processes. In this review, we summarize the regulatory mechanisms of Kcr and its functions in DDR, including its involvement in double-strand break (DSB)-induced transcriptional repression, DSB repair, and the DNA replication stress response.
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| http://dx.doi.org/10.3390/biom12101428 | DOI Listing |
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Article Synopsis
- A certain beneficial microorganism in the rhizosphere enhances plant growth and tolerance to salt stress, but the specific mechanisms at the post-translational modification level were not well understood.
- Researchers identified various lysine modifications, specifically noting that acetylation levels increased significantly in response to salt stress, affecting a large number of proteins involved in vital processes related to salt tolerance.
- The study also highlighted how specific acetylation sites on a protective enzyme, thiol peroxidase, play a crucial role in managing reactive oxygen species, thus influencing bacterial growth under salt conditions.
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