Limits...
The BLI-3/TSP-15/DOXA-1 dual oxidase complex is required for iodide toxicity in Caenorhabditis elegans.

Xu Z, Luo J, Li Y, Ma L - G3 (Bethesda) (2014)

Bottom Line: The C. elegans dual oxidase maturation factor DOXA-1 is also required for the arresting effect of excess iodide.Finally, we detected a dramatically increased biogenesis of reactive oxygen species in animals treated with excess iodide, and this effect can be partially suppressed by bli-3 and tsp-15 mutations.We propose that the BLI-3/TSP-15/DOXA-1 dual oxidase complex is required for the toxic pleiotropic effects of excess iodide.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Medical Genetics and School of Life Sciences, Central South University, Changsha, Hunan 410078, China.

Show MeSH

Related in: MedlinePlus

Some mac mutations affect bli-3 and tsp-15. (A) The mac mutations in bli-3 affect conserved (mac41: G44S, mac38: S694F) or nonconserved (mac40: A1263T, mac37: A1330V) amino acids in different domains of BLI-3. Nucleotide changes, amino acid changes, and BLI-3 DUOX1 partial sequence alignments of different species were presented. TM: transmembrane domain. (B) mac33 affects a nonconserved amino acid residue in the fourth transmembrane domain of TSP-15. Nucleotide change, amino acid change, and TSP-15 partial sequence alignment were presented.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4321028&req=5

fig3: Some mac mutations affect bli-3 and tsp-15. (A) The mac mutations in bli-3 affect conserved (mac41: G44S, mac38: S694F) or nonconserved (mac40: A1263T, mac37: A1330V) amino acids in different domains of BLI-3. Nucleotide changes, amino acid changes, and BLI-3 DUOX1 partial sequence alignments of different species were presented. TM: transmembrane domain. (B) mac33 affects a nonconserved amino acid residue in the fourth transmembrane domain of TSP-15. Nucleotide change, amino acid change, and TSP-15 partial sequence alignment were presented.

Mentions: We determined the coding sequences of bli-3 in the isolates of the mac40 complementation group and identified a missense mutation in each of the four mutants (Figure 3A). These mutations caused a G44S (mac41) change in the peroxidase domain, an S694F (mac38) change in the region between the first transmembrane domain and the EF hand domain, and an A1263T (mac40) change and an A1330V (mac37) change in the NADPH oxidase domain (Figure 3A).


The BLI-3/TSP-15/DOXA-1 dual oxidase complex is required for iodide toxicity in Caenorhabditis elegans.

Xu Z, Luo J, Li Y, Ma L - G3 (Bethesda) (2014)

Some mac mutations affect bli-3 and tsp-15. (A) The mac mutations in bli-3 affect conserved (mac41: G44S, mac38: S694F) or nonconserved (mac40: A1263T, mac37: A1330V) amino acids in different domains of BLI-3. Nucleotide changes, amino acid changes, and BLI-3 DUOX1 partial sequence alignments of different species were presented. TM: transmembrane domain. (B) mac33 affects a nonconserved amino acid residue in the fourth transmembrane domain of TSP-15. Nucleotide change, amino acid change, and TSP-15 partial sequence alignment were presented.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4321028&req=5

fig3: Some mac mutations affect bli-3 and tsp-15. (A) The mac mutations in bli-3 affect conserved (mac41: G44S, mac38: S694F) or nonconserved (mac40: A1263T, mac37: A1330V) amino acids in different domains of BLI-3. Nucleotide changes, amino acid changes, and BLI-3 DUOX1 partial sequence alignments of different species were presented. TM: transmembrane domain. (B) mac33 affects a nonconserved amino acid residue in the fourth transmembrane domain of TSP-15. Nucleotide change, amino acid change, and TSP-15 partial sequence alignment were presented.
Mentions: We determined the coding sequences of bli-3 in the isolates of the mac40 complementation group and identified a missense mutation in each of the four mutants (Figure 3A). These mutations caused a G44S (mac41) change in the peroxidase domain, an S694F (mac38) change in the region between the first transmembrane domain and the EF hand domain, and an A1263T (mac40) change and an A1330V (mac37) change in the NADPH oxidase domain (Figure 3A).

Bottom Line: The C. elegans dual oxidase maturation factor DOXA-1 is also required for the arresting effect of excess iodide.Finally, we detected a dramatically increased biogenesis of reactive oxygen species in animals treated with excess iodide, and this effect can be partially suppressed by bli-3 and tsp-15 mutations.We propose that the BLI-3/TSP-15/DOXA-1 dual oxidase complex is required for the toxic pleiotropic effects of excess iodide.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Medical Genetics and School of Life Sciences, Central South University, Changsha, Hunan 410078, China.

Show MeSH
Related in: MedlinePlus