Ordered assembly of mitochondria during rice germination begins with pro-mitochondrial structures rich in components of the protein import apparatus
Related Experiment Video
Updated: Aug 13, 2026

Rapid Isolation of the Mitoribosome from HEK Cells
Published on: October 4, 2018
Katharine A Howell1, A Harvey Millar, James Whelan
1ARC Centre of Excellence in Plant Energy Biology, CMS Building M310, University of Western Australia, 35 Stirling Hwy, Perth, WA 6009, Australia.
Abstract:
Mitochondrial maturation during imbibition of rice embryos follows the transition of unstructured double membrane bound pro-mitochondria to the typical cristae-rich mitochondrial structures observed in mature plant cells. During the first 48 h following imbibition, an ordered increase in the abundance of transcripts encoding mitochondrial proteins was observed. Co-incident with these changes in transcript levels was dynamic and rapid changes in mitochondrial protein content and mitochondrial function. Proteins representing components of the mitochondrial protein import apparatus are strikingly abundant in dry seeds, and a functional import apparatus was shown to operate 2 h after imbibition. Interestingly, this import process was best driven by the oxidation of NADH from outside the mitochondrial inner membrane. In later developmental stages the capacity for matrix organic acid metabolism was evident, accompanied by the appearance of proteins for TCA cycle components, and coordination of electron transport chain assembly through components encoded in both mitochondrial and nuclear genomes. Together these events provide new insights into the understanding of mitochondrial maturation and the nature of pro-mitochondrial structures in plant cells.
Related Concept Videos
Mitochondrial Protein Sorting
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Porin Insertion in the Outer Mitochondrial Membrane
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Structure of Porins
Mitochondrial Precursor Proteins
Most of the mitochondrial precursors...
Protein Transport into the Inner Mitochondrial Membrane
Transport of mitochondrial precursors across the TIM23 channel is driven by...

