The Dynamic Chondriome: Control of Number, Shape, Size and Motility of Mitochondria

Abstract

The important roles of mitochondrial fusion and fission in shaping chondriome structure were known at that time, only to be forgotten, or overlooked, over the next 80‐plus years until cell biology was rejuvenated by the application of fluorescent protein technology. The motility of plant mitochondria is necessary to enable the individual physically discrete mitochondria to interact and to fuse, and to facilitate redistribution of mitochondria within the cell. In contrast, disruption of the fusion apparatus, at least inS. cerevisiae, leads to an increase in the number of individual mitochondria together with a decreased volume of individual organelles. The interweaving of mitochondrial dynamics and mitochondrial quality control (MQC) is complex, and quality control (QC) involves fusion and fission in order to drive biogenesis, while fission is additionally required to isolate damaged mitochondria from the rest of the chondriome.

Single organelle function and organization as estimated from Arabidopsis mitochondrial proteomics

“…The balance between mitochondrial fusion and fission events controls mitochondrial genome distribution, mitochondrial size, shape and number within a cell, and mitochondrial segregation between the daughter cells during cell division (Arimura et al ., 2004b; Sheahan et al ., , ; Logan and Paszkiewicz, ). While the genetic components of the fusion machinery are unknown in plants, several proteins involved in fission have been identified (Arimura et al ., 2004b; Logan and Paszkiewicz, ).…”

“…The balance between mitochondrial fusion and fission events controls mitochondrial genome distribution, mitochondrial size, shape and number within a cell, and mitochondrial segregation between the daughter cells during cell division (Arimura et al ., 2004b; Sheahan et al ., , ; Logan and Paszkiewicz, ). While the genetic components of the fusion machinery are unknown in plants, several proteins involved in fission have been identified (Arimura et al ., 2004b; Logan and Paszkiewicz, ). All established components of the fission machinery were found in the proteomic dataset (Figure ; Dataset S2, worksheet #12), with the exception of Fission1b (FIS1B) and Elongated mitochondria 2 (ELM2), whose contribution in the mitochondrial division seems to be marginal (Arimura et al ., ), and FRIENDLY, which is a cytosolic protein only transiently associated with the mitochondria (El Zawily et al ., ).…”