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Article Navigation >  Journal of Genetics and Genomics  > 2026  > Accepted Manuscript

Natural variation in Miniature5 determines mitochondrial nad1 splicing and seed development in maize

doi: 10.1016/j.jgg.2026.03.021
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    a. State Key Laboratory of High-Efficiency Production of Wheat-Maize Double Cropping, CIMMYT-Henan Joint Center for Wheat and Maize Improvement, Collaborative Innovation Center of Henan Grain Crops, College of Agronomy, Henan Agricultural University, Zhengzhou, Henan 450002, China;

  •  

    b. The Shennong Laboratory, Zhengzhou, Henan 450002, China

Funds:

We thank Dr. Xiaoduo Lu (Qilu Normal University) for providing the maize EMS mutant line and Ms. Lina Xu for technical support with cytological analysis. This research was supported by the National Key Research and Development Program of China (2021YFF1000304) and the Natural Science Foundation of Henan for Excellent Young Scholars (232300421035) awarded to QS

and the Key Scientific and Technological Project of Henan Province Department of China (232102111108) awarded to HC.

the China Postdoctoral Science Foundation (2023M741064) to awarded JL

the National Key Research and Development Program of China (2021YFF1000303) and the National Natural Science Foundation of China (U22A20466 and 32472118) awarded to GW

  • Received Date: 2025-11-05
  • Accepted Date: 2026-03-25
  • Rev Recd Date: 2026-03-17
    • Available Online: 2026-04-01
    Abstract
  • Seed size is a key determinant of cereal grain yield, but natural variations in defective-kernel genes have rarely been applied in maize breeding. Here, we report the positional cloning of maize Miniature5 (Mn5), which encodes a mitochondrial-targeted P-class pentatricopeptide repeat (PPR) protein. Further analysis shows that a missense mutation of mn5, Mn5Val109, presents in maize populations and correlates with reduced seed size. The Mn5Val109 variant exhibits compromised function in the mn5-ref mutant, failing to trans-splice mitochondrial nad1 intron1, drastically reducing the abundance and activity of respiratory complex I, accompanied by disorganized mitochondrial cristae. Mn5 directly binds to domain IV of the pre-nad1.1 transcript. Notably, this binding site is located downstream of the previously presumed 3′-terminus bound by MITOCHONDRIA STABILITY/PROCESSING PPR FACTOR1 (MSP1), thus redefining the 3′-end of the nad1.1 pre-RNA. Furthermore, Mn5 physically interacts with the maturases ZmnMAT1 and ZmnMAT3, as well as the PPR proteins PPR-SMR1 and SPR2, which are broadly involved in organellar group II intron splicing. Together, our results suggest that Mn5 recruits maturases and PPR proteins to form spliceosomal complexes responsible for the trans-splicing of nad1 intron1. Importantly, natural variations in Mn5 confer differences in seed size control, offering potential for breeding high-yield maize varieties.
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