español    español

Biosynthesis of cofactor activatable iron-only nitrogenase in Saccharomyces cerevisiae

Engineering nitrogenase in eukaryotes is hampered by its genetic complexity and by the oxygen sensitivity of its protein components. Of the three types of nitrogenases, the Fe-only nitrogenase is considered the simplest one because its function depends on fewer gene products than the homologous and more complex Mo and V nitrogenases. In this work, CBGP researches show the expression of stable Fe-only
nitrogenase component proteins in the low-oxygen mitochondria matrix of S. cerevisiae. As-isolated Fe protein (AnfH) was active in electron donation to NifDK to reduce acetylene into ethylene. Ancillary proteins NifU, NifS andNifM were not required for Fe protein function. The FeFe protein existed as apo-AnfDK complex with the AnfG subunit either loosely bound or completelyunable to interact with it. Apo-AnfDK could be activated for acetylene reduction by the simple addition of FeMo-co in vitro, indicating preexistence of the P-clusters even in the absence of coexpressed NifU and NifS. This work reinforces the use of Fe-only nitrogenase as simple model to engineer nitrogen fixation in yeast and plant mitochondria.

zoom

Original Paper:

López‐Torrejón, G., Burén, S., Veldhuizen, M., Rubio, L.M. 2021. Biosynthesis of cofactor-activatable iron-only nitrogenase in Saccharomyces cerevisiae. Microbial Biotechnology. DOI: https://doi.org/10.1111/1751-7915.13758

Centre for Plant Biotechnology and Genomics UPM – INIA Parque Científico y Tecnológico de la U.P.M. Campus de Montegancedo
Autopista M-40, Km 38 - 28223 Pozuelo de Alarcón (Madrid) Tel.: +34 91 0679100 ext. 79100 Fax: +34 91 7157721. Location and Contact

Síguenos en: