ArticleJournal of bioenergetics and biomembranes2006
Caenorhabditis elegans MAI-1 protein, which is similar to mitochondrial ATPase inhibitor (IF1), can inhibit yeast F0F1-ATPase but cannot be transported to yeast mitochondria.
Article in Journal of bioenergetics and biomembranes, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- A cytosolic IF1 reporter enables real-time visualization of severe mitochondrial membrane damage.The Journal of cell biology · 2026Article
- A genetic screen identifiesmicroPublication biology · 2024Article
- Bacterial peptidoglycan muropeptides benefit mitochondrial homeostasis and animal physiology by acting as ATP synthase agonists.Developmental cell · 2022Article
- The F1Fo-ATPase inhibitor protein IF1 in pathophysiology.Frontiers in physiology · 2022Review
- Trypanosoma brucei TbIF1 inhibits the essential F1-ATPase in the infectious form of the parasite.PLoS neglected tropical diseases · 2017Article
- miRNAs cooperate in apoptosis regulation duringGenes & development · 2017Article
- Article
- The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution.Journal of bioenergetics and biomembranes · 2015Article
- The shrimp mitochondrial FoF1-ATPase inhibitory factor 1 (IF1).Journal of bioenergetics and biomembranes · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
In Caenorhabditis elegans, two proteins that are similar to mitochondrial ATPase inhibitor protein (IF(1)) have been found and named MAI-1 and MAI-2. In this study, we overexpressed and purified both the proteins and examined their properties. Circular dichroism spectra indicated that both the MAI-1 and MAI-2 predominantly consisted of beta- and random structure, and in contrast to mammalian IF(1), alpha-helixes were barely detected. Both MAI-1 and MAI-2 could inhibit yeast F(0)F(1)-ATPase, but the inhibition by MAI-1 was pH-independent. MAI-2-GFP fusion protein was transported to yeast mitochondria, but MAI-1-GFP was not. These results indicate that the MAI-2 is (C. elegans) IF(1). MAI-1 seems to be a cytosolic protein and may regulate cytosolic ATPase(s).
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