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Article

Differential effects of two catalytic mutations on full-length PRDM9 and its isolated PR/SET domain reveal a case of pseudomodularity.

Genetics - 10 Dec 2021

Powers Natalie R, Billings Timothy, Paigen Kenneth, Petkov Petko M

Abstract excerpt

PRDM9 is a DNA-binding histone methyltransferase that designates and activates recombination hotspots in mammals by locally trimethylating lysines 4 and 36 of histone H3. In mice, we recently reported two independently produced point mutations at the same residue, Glu360Pro (Prdm9EP) and Glu360Lys (Prdm9EK), which severely reduce its H3K4 and H3K36 methyltransferase activities in vivo. Prdm9EP is slightly less...

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Identifiers

PMID: 34747456
DOI: 10.1093/genetics/iyab172
PMCID: PMC8664581

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