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PMID:17698960
| Citation |
Chen, XJ, Wang, X and Butow, RA (2007) Yeast aconitase binds and provides metabolically coupled protection to mitochondrial DNA. Proc. Natl. Acad. Sci. U.S.A. 104:13738-43 |
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| Abstract |
Aconitase (Aco1p) is a multifunctional protein: It is an enzyme of the tricarboxylic acid cycle. In animal cells, Aco1p also is a cytosolic protein binding to mRNAs to regulate iron metabolism. In yeast, Aco1p was identified as a component of mtDNA nucleoids. Here we show that yeast Aco1p protects mtDNA from excessive accumulation of point mutations and ssDNA breaks and suppresses reductive recombination of mtDNA. Aconitase binds to both ds- and ssDNA, with a preference for GC-containing sequences. Therefore, mitochondria are opportunistic organelles that seize proteins, such as metabolic enzymes, for construction of the nucleoid, an mtDNA maintenance/segregation apparatus. |
| Links |
PubMed PMC1959452 Online version:10.1073/pnas.0703078104 |
| Keywords |
Aconitate Hydratase/chemistry; Aconitate Hydratase/genetics; Aconitate Hydratase/metabolism; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Repair/genetics; DNA, Mitochondrial/genetics; DNA, Mitochondrial/metabolism; DNA, Recombinant/genetics; DNA, Single-Stranded/genetics; Genome, Fungal/genetics; Models, Molecular; Mutation/genetics; Protein Binding; Protein Structure, Tertiary; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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