Biochemical study demonstrates how Eaf3 and Rco1 coordinate histone recognition in yeast, highlighting the molecular assembly of transcription-regulatory chromatin complexes.
In Saccharomyces cerevisiae , reduced potassium dependency-3 (Rpd3) resides in two distinct histone deacetylase complexes, termed Rpd3S and Rpd3L 1 , 2 , 3 . The Rpd3S complex functions to repress transcriptional initiation within the coding region of genes during RNA polymerase II elongation by maintaining hypoacetylation 2 , 4 . Eaf3 and Rco1 are unique members of Rpd3S. Eaf3 binds to di- and tri-methylation of histone H3 at lysine 36 (H3K36me2/3) via its N-terminal chromo barrel domain (Eaf3 CBD ) 5 , and it also resides in the NuA4 histone acetyltransferase complex 4 , 5 , 6 . Rco1 recognizes unmodified H3K4 (H3K4me0) via its PHD1 domain and associates with Eaf3 to enhance the Eaf3–H3K36me3 interaction 7 . Thus, H3K4me0 and H3K36me recognition by Rpd3S enforces the targeting and activity of Rpd3S within gene bodies that are rich in H3K36 methylation but depleted in H3K4 methylation 8 . However, the underlying molecular mechanisms of Eaf3–Rco1 interaction are largely unknown.
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Chen et al. (2023) studied this question.
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