Cloning and expression of a heme binding protein from the genome of Saccharomyces cerevisiae

Karine Auclair, Hong Wei Huang, Pierre Moënne-Loccoz, Paul R. Ortiz De Montellano

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The YLR205c gene of Saccharomyces cerevisiae does not show significant sequence identity to any known gene, except for heme oxygenase (22% to human HO-1). The YLR205 ORF was cloned and overexpressed in both Escherichia coli and S. cerevisiae. Both expression systems yielded proteins that bound heme tightly. The isolated YLR205c protein underwent reduction in the presence of either NADPH-cytochrome P450 reductase or NADH-putidaredoxin-putidaredoxin reductase but did not exhibit heme oxygenase activity. The protein exhibited modest H2O2-dependent peroxidase activities with guaiacol, potassium iodide, and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS). Thus, YLR205c codes for a hemoprotein of unkown physiological function that exhibits peroxidase activity.

Original languageEnglish (US)
Pages (from-to)340-349
Number of pages10
JournalProtein Expression and Purification
Volume28
Issue number2
DOIs
StatePublished - Apr 1 2003

ASJC Scopus subject areas

  • Biotechnology

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