ArticleYeast (Chichester, England)2021
Absence of MMF1 disrupts heme biosynthesis by targeting Hem1pin Saccharomyces cerevisiae.
Article in Yeast (Chichester, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- Perturbation of the MetJ regulon impacts the consequences of 2-aminoacrylate stress inMicrobiology (Reading, England) · 2025Article
- Tetrahydrofolate levels influence 2-aminoacrylate stress inJournal of bacteriology · 2024Article
- RidA proteins contribute to fitness ofMicrobial cell (Graz, Austria) · 2024Article
- Modulators of a robust and efficient metabolism: Perspective and insights from the Rid superfamily of proteins.Advances in microbial physiology · 2023Review
- DadY (PA5303) is required for fitness ofMicrobial cell (Graz, Austria) · 2022Article
- Article
- 2-Aminoacrylate stress damages diverse PLP-dependent enzymes in vivo.The Journal of biological chemistry · 2022Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The RidA subfamily of the Rid (YjgF/YER057c/UK114) superfamily of proteins is broadly distributed and found in all domains of life. RidA proteins are enamine/imine deaminases. In the organisms that have been investigated, lack of RidA results in accumulation of the reactive enamine species 2-aminoacrylate (2AA) and/or its derivative imine 2-iminopropanoate (2IP). The accumulated enamine/imine species can damage specific pyridoxal phosphate (PLP)-dependent target enzymes. The metabolic imbalance resulting from the damaged enzymes is organism specific and based on metabolic network configuration. Saccharomyces cerevisiae encodes two RidA homologs, one localized to the cytosol and one to the mitochondria. The mitochondrial RidA homolog, Mmf1p, prevents enamine/imine stress and is important for normal growth and maintenance of mitochondrial DNA. Here, we show that Mmf1p is necessary for optimal heme biosynthesis. Biochemical and/or genetic data herein support a model in which accumulation of 2AA and or 2IP, in the absence of Mmf1p, inactivates Hem1p, a mitochondrially located PLP-dependent enzyme required for heme biosynthesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.