Exploiting genetic diversity and gene synthesis to identify superior nitrogenase NifH protein variants to engineer N2-fixation in plants

Jiang, Xi and Payá Tormo, Lucía and Coroian, Diana María and García Rubio, Inés and Castellanos Rueda, Rocío and Eseverri Sabaté, Álvaro and López Torrejón, Gema and Burén, Stefan and Rubio Herrero, Luis Manuel (2021). Exploiting genetic diversity and gene synthesis to identify superior nitrogenase NifH protein variants to engineer N2-fixation in plants. "Communications Biology" (n. 4); p. 4. ISSN 2399-3642. https://doi.org/10.1038/s42003-020-01536-6.

Description

Title: Exploiting genetic diversity and gene synthesis to identify superior nitrogenase NifH protein variants to engineer N2-fixation in plants
Author/s:
  • Jiang, Xi
  • Payá Tormo, Lucía
  • Coroian, Diana María
  • García Rubio, Inés
  • Castellanos Rueda, Rocío
  • Eseverri Sabaté, Álvaro
  • López Torrejón, Gema
  • Burén, Stefan
  • Rubio Herrero, Luis Manuel
Item Type: Article
Título de Revista/Publicación: Communications Biology
Date: January 2021
ISSN: 2399-3642
Subjects:
Faculty: Centro de Investigación en Biotecnología y Genómica de Plantas (CBGP) (UPM)
Department: Otro
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Engineering nitrogen fixation in eukaryotes requires high expression of functional nitrogenase structural proteins, a goal that has not yet been achieved. Here we build a knowledge-based library containing 32 nitrogenase nifH sequences from prokaryotes of diverse ecological niches and metabolic features and combine with rapid screening in tobacco to identify superior NifH variants for plant mitochondria expression. Three NifH variants outperform in tobacco mitochondria and are further tested in yeast. Hydrogenobacter thermophilus (Aquificae) NifH is isolated in large quantities from yeast mitochondria and fulfills NifH protein requirements for efficient N2 fixation, including electron transfer for substrate reduction, P-cluster maturation, and FeMo-co biosynthesis. H. thermophilus NifH expressed in tobacco leaves shows lower nitrogenase activity than that from yeast. However, transfer of [Fe4S4] clusters from NifU to NifH in vitro increases 10-fold the activity of the tobacco-isolated NifH, revealing that plant mitochondria [Fe-S] cluster availability constitutes a bottleneck to engineer plant nitrogenases.

Funding Projects

TypeCodeAcronymLeaderTitle
Government of SpainFPU16/02284UnspecifiedUnspecifiedUnspecified
Government of SpainCTQ2015-64486-RUnspecifiedUnspecifiedCatalizadores de oxigenación y de oxidación de agua

More information

Item ID: 65934
DC Identifier: https://oa.upm.es/65934/
OAI Identifier: oai:oa.upm.es:65934
DOI: 10.1038/s42003-020-01536-6
Official URL: https://www.nature.com/articles/s42003-020-01536-6
Deposited by: Memoria Investigacion
Deposited on: 20 Apr 2021 07:40
Last Modified: 20 Apr 2021 07:40
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