Biosynthesis of the nitrogenase active-site cofactor precursor NifB-co in Saccharomyces cerevisiae
Abstract
Nitrogen is a constituent of many essential biomolecules and plentiful on earth as inert N 2 gas. For its assimilation by eukaryotes, N 2 must be converted to a metabolically tractable form such as ammonium. Such conversion is catalyzed by nitrogenase, an enzyme produced by a select group of microorganisms called diazotrophs. Crop yields necessary to feed the world's population have critically depended on applying nitrogenous fertilizers. Incorporation of prokaryotic determinates required to produce active nitrogenase into crop plants would have enormous economic and environmental benefits. The active-site cofactors of all nitrogenases have a common metallocluster precursor synthesized by NifB. Here, we identify the genetic determinants for NifB function in mitochondria of Saccharomyces cerevisiae , thereby advancing prospects to generate N 2 -fixing crops.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Nov 25, 2019
- Source ID
- 10.1073/pnas.1904903116
Entities
People
- Ben Gordon
- Carlos Echavarri-Erasun
- Christopher Voigt
- Dennis R Dean
- Emilio Jimenez-Vicente
- Ishtiaq Saaem
- Katelin Pratt
- Luis M. Rubio
- Stefan Burén
- Xi Jiang
- Yisong Guo
Organizations
- Broad Institute
- Carnegie Mellon University
- Gates Foundation
- Massachusetts Institute of Technology
- Technical University of Madrid
- Virginia Tech