Isolation of a cytochrome aa3 gene from Bradyrhizobium japonicum
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منابع مشابه
Isolation of a cytochrome aa(3) gene from Bradyrhizobium japonicum.
Bradyhizobium japonicum strain LO501 is a Tn5-induced mutant that does not express the terminal oxidase cytochrome aa(3) (cytochrome-c oxidase, EC 1.9.3.1). Two and one-half kilobase pairs of LO501 genomic DNA that flanks the transposon was isolated and used as a hybridization probe to obtain the wild-type gene from a cosmid library. Two subcloned fragments from two of the isolated cosmids were...
متن کاملIsolation and characterization of the lipopolysaccharides from Bradyrhizobium japonicum.
The lipopolysaccharide (LPS) of Bradyrhizobium japonicum 61A123 was isolated and partially characterized. Phenol-water extraction of strain 61A123 yielded LPS exclusively in the phenol phase. The water phase contained low-molecular-weight glucans and extracellular or capsular polysaccharides. The LPSs from B. japonicum 61A76, 61A135, and 61A101C were also extracted exclusively into the phenol p...
متن کاملIsolation and Characterization of a Competition-Defective Bradyrhizobium japonicum Mutant.
Tn5 mutagenesis was coupled with a competition assay to isolate mutants of Bradyrhizobium japonicum defective in competitive nodulation. A double selection procedure was used, screening first for altered extracellular polysaccharide production (nonmucoid colony morphology) and then for decreased competitive ability. One mutant, which was examined in detail, was deficient in acidic polysaccharid...
متن کاملCytochrome aa3 from Nitrosomonas europaea.
Cytochrome c oxidase has been purified from the ammonia oxidizing chemoautotroph Nitrosomonas europaea by ion-exchange chromatography in the presence of Triton X-100. The enzyme has absorption maxima at 420 and 592 nm in the resting state and at 444 and 598 nm in the dithionite-reduced form; optical extinction coefficient (598 nm minus 640 nm) = 21.9 cm-1 nM-1. The enzyme has approximately 11 n...
متن کاملThe Bradyrhizobium japonicum cycM gene encodes a membrane-anchored homolog of mitochondrial cytochrome c.
Mitochondrial cytochrome c is a water-soluble protein in the intermembrane space which catalyzes electron transfer from the cytochrome bc1 complex to the terminal oxidase cytochrome aa3. In Bradyrhizobium japonicum, a gene (cycM) which apparently encodes a membrane-anchored homolog of mitochondrial cytochrome c was discovered. The apoprotein deduced from the nucleotide sequence of the cycM gene...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1987
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.84.10.3219