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These EGTs represent a cell division component, a rhamnose-proton symporter and a DNA-damage-inducible protein.
Suppression of mtDNA loss from fzo1 ∆ aac2 ∆ cells by the PDR1 -249 allele was compared to the suppression mediated by deletion of a gene encoding a known mitochondrial division component for S. cerevisiae, FIS1.
Some sfa alleles exhibited noncomplementation when combined with more than one division component, perhaps due to the reported unlinked noncomplementation of certain mutations affecting mitochondrial division (Tieu and Nunnari 2000) and also were not studied further.
Cells lacking the mitochondrial division component Fis1p, however, were not resistant to these agents, and even exhibited increased sensitivity to CHX, demonstrating that not all mutations permitting mtDNA maintenance by fzo1 ∆ aac2 ∆ cells lead to PDR activation.
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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.
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