Arabidopsis histone acetyltransferase complex coordinates cytoplasmic histone acetylation and nuclear chromatin accessibility.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39630902.
- Also identified by DOI 10.1126/sciadv.adp1840 and PMC identifier 11616720.
- Licence recorded as CC BY-NC.
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Abstract
Conserved type B histone acetyltransferases are recognized for their role in acetylating newly synthesized histones in the cytoplasm of eukaryotes. However, their involvement in regulating chromatin within the nucleus remains unclear. Our study shows that the <i>Arabidopsis thaliana</i> type B histone acetyltransferase HAG2 interacts with the histone chaperones MSI2, MSI3, and NASP, as well as the histones H3 and H4, forming a complex in both the cytoplasm and the nucleus. Within this complex, HAG2 and MSI2/3 constitute a histone acetylation module essential for acetylating histone H4 in the cytoplasm. Furthermore, this module works together with NASP to regulate histone acetylation, chromatin accessibility, and gene transcription in the nucleus. This complex enhances chromatin accessibility near transcription start sites while reducing accessibility near transcription termination sites. Our findings reveal a distinct role for the <i>Arabidopsis</i> type B histone acetyltransferase in the nucleus, shedding light on the coordination between cytoplasmic histone acetylation and nuclear chromatin regulation in plants.
Medical subject headings
- Arabidopsis
- Histone Acetyltransferases
- Histones
- Chromatin
- Arabidopsis Proteins
- Cell Nucleus
- Cytoplasm