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Copper Metallochaperones are Required for the Assembly of Bacteroid Cytochrome c Oxidase Which is Functioning for Nitrogen Fixation in Soybean Nodules
Author(s) -
Hatthaya Arunothayanan,
Mika Nomura,
Rie Hamaguchi,
Manabu Itakura,
Kiwamu Minamisawa,
Shigeyuki Tajima
Publication year - 2010
Publication title -
plant and cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.975
H-Index - 152
eISSN - 1471-9053
pISSN - 0032-0781
DOI - 10.1093/pcp/pcq079
Subject(s) - cytochrome c oxidase , nitrogen fixation , bradyrhizobium japonicum , mutant , electron transport chain , electron transport complex iv , biochemistry , cytochrome c , chemistry , cytochrome , oxidase test , biology , bacteria , gene , enzyme , rhizobiaceae , genetics , mitochondrion , symbiosis
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)X(10)MX(21)HXM. 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.

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