Histone acetyltransferase KAT7 is associated with mitochondrial function during porcine oocyte maturation

The MYST family of lysine acetyltransferase (KAT) are required for many critical nuclear functions, including transcription and DNA damage repair in somatic cells; however, the functions of individual MYST members in mammalian oocyte meiosis remain largely unclear. Here, we show that KAT7, as a key MYST family member, might support mitochondrial function during porcine oocyte maturation. We found that KAT7 localized to the cytoplasm during meiotic progression. Moreover, impaired oocyte maturation was observed following its inhibition, which was associated with compromised mitochondrial ATP production and elevated oxidative stress. In addition, TUFM, a mitochondrial translation elongation factor essential for the synthesis of electron transport chain subunits, was downregulated following KAT7 inhibition. Consistently, COX1, a subunit of complex IV, was downregulated and the NADH/NAD⁺ redox balance was disrupted. Collectively, these findings suggest a role for KAT7 in mitochondrial function, potentially through its association with ETC-related events during oocyte maturation.