AI Article Synopsis
- Methylation of histone H3 lysine 4 (H3K4) is associated with active gene transcription and can be modified by various proteins, including LSD1 and JmjC domain proteins.
- The study identifies lysyl oxidase-like 2 (LOXL2) as a new player that deaminates trimethylated H3K4, introducing a unique chemical modification mechanism for this histone mark.
- LOXL2's impact on H3K4me3 deamination is linked to the transcription regulation of the CDH1 gene, indicating additional complexity in histone modification processes.
Article Abstract
Unlabelled: Methylation of histone H3 lysine 4 is linked to active transcription and can be removed by LSD1 or the JmjC domain-containing proteins by amino-oxidation or hydroxylation, respectively. Here we describe that its deamination can be catalyzed by lysyl oxidase-like 2 protein (LOXL2), presenting an unconventional chemical mechanism for H3K4 modification. Infrared spectroscopy and mass spectrometry analyses demonstrated that recombinant LOXL2 specifically deaminates trimethylated H3K4. Moreover, by regulating H3K4me3 deamination, LOXL2 activity is linked with the transcriptional control of the CDH1 gene. These results reveal the existence of further H3 modification as well as a novel mechanism for H3K4me3 demethylation.
Database: The GEO accession number for the data referred to this paper is GSE35600.
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| http://dx.doi.org/10.1111/febs.13922 | DOI Listing |
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