Cell Biology of the Mitochondrion

Abstract

In the article by A. M. van der Bliek, M. M. Sedensky, and P. G. Morgan entitled "Cell Biology of the Mitochondrion" on page 855, the second full paragraph incorrectly attributed the development of a luciferase-expressing strain in Caenorhabditis elegans to the Meyer laboratory. The sentence beginning "Perhaps most importantly. . ." was deleted and replaced with the following sentences:"In the Glover and Pettitt laboratories, Lagido et al. (2008) developed a luciferase-expressing strain that allowed in vivo assessment of relative ATP levels in C. elegans. They later described the use of this strain for monitoring toxicant effects on mitochondrial function (McLaggan et al. 2012; Lagido et al. 2015). Members from the Meyer laboratory extended the use of this strain to allow rapid evaluation of the effects of toxicants on mitochondrial function, particularly the electron transport chain, glycolysis, and fatty acid oxidation (Luz et al. 2016b)."The following references were added to the Literature Cited section:

ROS-based lethality ofC. elegansmitochondrial electron transport mutants grown onE. colisiderophore iron release mutants

“…Previous C. elegans RNAi screens have shown that many mitochondrial gene inactivations are lethal (Rea et al, 2007). However, viable reduction-of-function mutants have been characterized (van der Bliek et al, 2017). We tested a viable spg-7(ad2249) mutant (Zubovych et al, 2010).…”

“…C. elegans nduf-7(et19), isp-1(qm150), and clk-1(qm30) mutant animals grown on the E. coli Δfes::kan mutant also dramatically arrest as L1 larvae (Table 3; Figure S5) while particular other C. elegans mitochondrial mutants including gas-1(fc21), nduf-2.2(ok2397), nuo-6(qm200), mev-1(kn1), and ucr-2.3(pk732) did not arrest when grown on the E. coli Δfes::kan mutant (Table 3; Figure S5). nduf-7(et19) is a partial loss-offunction mutation in nduf-7 (NADH-ubiquinone oxidoreductase Fe-S), a subunit of the mitochondrial electron transport chain complex I (Rauthan et al, 2015;van der Bliek et al, 2017). nduf-7(et19) mutant animals strongly activate UPR mt , have a reduced respiration rate and longer lifespan (Rauthan et al, 2015).…”

“…isp-1(qm150) mutants have lower oxygen consumption, decreased ROS production, and increased lifespan (Feng et al, 2001). clk-1 encodes an ortholog of the highly conserved demethoxyubiquinone (DMQ) hydroxylase that is necessary for ubiquinone biosynthesis (van der Bliek et al, 2017). Mutations in C. elegans clk-1 causes slow development, reduced respiration, and increased lifespan when grown on an E. coli strain that is competent to produce bacterial ubiquinone that is identical except for a shorter isoprenoid chain that localizes this electron carrier to the membrane (Felkai et al, 1999).…”

“…S5). nduf-7(et19) is a partial loss-of-function mutation in nduf-7 (NADH-ubiquinone oxidoreductase Fe-S), a subunit of the mitochondrial electron transport chain complex I (11,22). nduf-7(et19) mutant animals strongly activate UPR mt , have a reduced respiration rate and longer lifespan (22).…”

Alcohol induces mitochondrial fragmentation and stress responses to maintain normal muscle function in Caenorhabditis elegans

“…Mitochondrial fission is mediated by the dynaminrelated protein DRP1. DRP1 is recruited to the outer mitochondrial membrane via its receptor proteins, such as Fis1 and Mff, assembles into spirals to wrap around the circumference of mitochondria, and split the membranes into two through constriction (6) Mitochondrial fusion is also facilitated by dynamin family proteins. Whereas outer membrane fusion is mediated by the Mitofusins Mfn1 and Mfn2 (FZO-1 in C. elegans), inner membrane fusion is mediated by Opa1 (EAT-3 in C. elegans).…”