biostudies-literatureWang CUS National Science FoundationNational Natural Science Foundation of Chinae2213540119https://www.ebi.ac.uk/biostudies/studies/S-EPMC9618065biostudies-literatureUnknown119(43)Heterochromatin is essential for genomic integrity and stability in eukaryotes. The mechanisms that regulate meiotic heterochromatin formation remain largely undefined. Here, we show that the catalytic subunit (POL2A) of <i>Arabidopsis</i> DNA polymerase epsilon (POL ε) is required for proper formation of meiotic heterochromatin. The POL2A N terminus interacts with the GHKL adenosine triphosphatase (ATPase) MORC1 (Microrchidia 1), and POL2A is required for MORC1's localization on meiotic heterochromatin. Mutations affecting the POL2A N terminus cause aberrant morphology of meiotic heterochromatin, which is also observed in <i>morc1</i>. Moreover, the POL2A C-terminal zinc finger domain (ZF1) specifically binds to histone H3.1-H4 dimer or tetramer and is important for meiotic heterochromatiProceedings of the National Academy of Sciences of the United States of AmericaDNA polymerase epsilon binds histone H3.1-H4 and recruits MORC1 to mediate meiotic heterochromatin condensation.PMC9618065IOS-1844264318702933200024631925005Li YHe CHuang JZhang JLi TWang CMa HJiang DCopenhaver GPDong AWang YfalseDNA polymerase epsilon binds histone H3.1-H4 and recruits MORC1 to mediate meiotic heterochromatin condensation.Heterochromatin is essential for genomic integrity and stability in eukaryotes. The mechanisms that regulate meiotic heterochromatin formation remain largely undefined. Here, we show that the catalytic subunit (POL2A) of <i>Arabidopsis</i> DNA polymerase epsilon (POL ε) is required for proper formation of meiotic heterochromatin. The POL2A N terminus interacts with the GHKL adenosine triphosphatase (ATPase) MORC1 (Microrchidia 1), and POL2A is required for MORC1's localization on meiotic heterochromatin. Mutations affecting the POL2A N terminus cause aberrant morphology of meiotic heterochromatin, which is also observed in <i>morc1</i>. Moreover, the POL2A C-terminal zinc finger domain (ZF1) specifically binds to histone H3.1-H4 dimer or tetramer and is important for meiotic heterochromati2022-01-01T00:00:00Z2022 Oct2025-04-04T08:29:12.535Z2025-04-04T08:29:12.535ZS-EPMC96180653626074310.1073/pnas.2213540119