ArticleThe Biochemical journal2003
Cytosolic iron superoxide dismutase is a part of the triacylglycerol biosynthetic complex in oleaginous yeast.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 13 citations in OpenAlex.
- Oversynthesis of riboflavin in the yeast Pichia guilliermondii is accompanied by reduced catalase and superoxide dismutases activities.Current microbiology · 2013Article
- Deleting the 14-3-3 protein Bmh1 extends life span in Saccharomyces cerevisiae by increasing stress response.Genetics · 2009Article
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4 authors at 1 institution in 1 country.
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Abstract
A novel multienzyme complex for the biosynthesis of triacylglycerol in oleaginous yeast has been identified recently in the cytosol and characterized [Gangar, Karande and Rajasekharan (2001) J. Biol. Chem. 276, 10290-10298]. Screening the library of Rhodotorula glutinis with an oligonucleotide probe derived from the N-terminal sequence of one of the protein components in the complex (21 kDa protein) resulted in the isolation of a 0.7 kb cDNA. Nucleotide sequence analysis revealed that the isolated gene codes for superoxide dismutase (SOD). Atomic absorption spectroscopy and inhibition assays showed that this cytosolic SOD utilizes Fe as its cofactor. Enzymic assays, immunoprecipitation and cross-linking experiments revealed that SOD is a part of the triacylglycerol biosynthetic complex, which could protect the substrate and the complex from oxidative damages. These results indicate for the first time the presence of iron-containing SOD in a soluble form in yeast.
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