Diverse cell division components interact with FtsZ to regulate FtsZ assembly.
In contrast, mitochondria, which are evolutionarily much older than chloroplasts, lost division components of bacterial origin with the exception of those present in primitive eukaryotes, which retained the Z ring.
These organelles share metabolic enzymes, division components, and very recently a novel vesicular mitochondrion-to-peroxisome pathway has been characterized [33], the physiological function of which is not understood.
Later, it became apparent that some sfa alleles originally classified as recessive suppressors were actually dominant in nature, yet provided weaker suppression than mutations of known division components.
Twenty-nine sfallele-containingng isolates either provided inconsistent results among different complementation tests or, alternatively, demonstrated noncomplementation of the suppressor mutation by multiple deletions of division components.
Consistent with this model, the association of ER tubules with mitochondrial constriction sites is independent of mitochondrial division components (Friedman et al., 2011).
Moreover, in contrast to key division components such as DLP1, Fis1 or Mff, mitochondrial fusion proteins were not localized to peroxisomes.
In the last decade, a number of cell division components involved in chromosome condensation, sister chromatid/homologous chromosome cohesion, kinetochore-spindle attachment/alignment, and cytokinesis have been identified.
These sites are enriched in mitochondrial division components, such as dynamin-related guanosine triphosphatases 1 (DRP1) and membrane protein mitochondrial fission factor (Mff) (Friedman et al. 2011; Youle and van der Bliek 2012).
Next-generation sequencing revealed that all identified suppressor mutations not associated with known mitochondrial division components were localized to PDR1 or PDR3, which encode transcription factors promoting drug resistance.
