Copper Metallochaperones are Required for the Assembly of Bacteroid Cytochrome c Oxidase Which is Functioning for Nitrogen Fixation in Soybean Nodules

• Published in: Plant and cell physiology Vol. 51; no. 7; pp. 1242 - 1246
• Main Authors: Arunothayanan, Hatthaya, Nomura, Mika, Hamaguchi, Rie, Itakura, Manabu, Minamisawa, Kiwamu, Tajima, Shigeyuki
• Format: Journal Article
• Language: English
• Published: Japan Oxford University Press 01-07-2010
• Subjects: Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bradyrhizobium - genetics; Bradyrhizobium - metabolism; Bradyrhizobium japonicum; Copper - metabolism; Cytochrome c oxidase; Electron Transport Complex IV - metabolism; Glycine max; Glycine max - microbiology; Metallochaperone; Metallochaperones - genetics; Metallochaperones - metabolism; Mutagenesis, Insertional; Mutation; Nitrogen Fixation; Root Nodules, Plant - microbiology
• ISSN: 0032-0781; 1471-9053
• DOI: 10.1093/pcp/pcq079

Bradyrhizobium japonicum, a symbiotic nitrogen-fixing bacterium for Glycine max, has complex respiratory electron transport chains. Bll4880 contained a copper-binding motif for metallochaperone, H(M)X₁₀MX₂₁HXM. A mutant strain, Bj4880, induced nodules with lower acetylene reduction activity. A double mutant, Bj4880-1131, which had inserted mutations both in blr1131, a gene of the Sco1-like protein, and in bll4880, induced nodules of significant Fix⁻ phenotype and low cytochrome c oxidase (Cco) activity in the bacteroid. Our data suggest that bll4880 protein is involved in copper ion delivery to Cco through blr1131 protein, and the expression of both proteins was induced under microaerobic conditions.