Cytosolic iron superoxide dismutase is a part of the triacylglycerol biosynthetic complex in oleaginous yeast

Sumana Raychaudhuri, Mamatha M. Reddy, Naveen R. Rajkumar, Ram Rajasekharan

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)587-594
Number of pages8
JournalBiochemical Journal
Volume372
Issue number2
DOIs
StatePublished - Jun 1 2003

Keywords

  • Acyl-carrier protein
  • Fatty acid activation
  • Iron superoxide dismutase
  • Rhodotorula glutinis
  • Triacylglycerol biosynthetic complex

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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