Characterization of an Azospirillum brasilense Tn5 mutant with enhanced N2 fixation: the effect of ORF280 on nifH expression

Disruption of an open reading frame (ORF) of 840 bp (280 amino acids; ORF280) in an Azospirillum brasilense Tn5 mutant resulted in a pleiotrophic phenotype. Besides an enhanced N2-fixing capacity and altered expression pattern of a nifH-gusA fusion, growth on the charged polar amino acids glutamate...

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Bibliographic Details
Published in:FEMS microbiology letters 2000-02, Vol.183 (1), p.23-29
Main Authors: Revers, L.F, Passaglia, L.M.P, Marchal, K, Frazzon, J, Blaha, C.G, Vanderleyden, J, Schrank, I.S
Format: Article
Language:English
Subjects:
Amino acids
Arginine
Azospirillum brasilense
Bacteriology
Biological and medical sciences
Bradyrhizobium japonicum
C-Terminus
Disruption
Fundamental and applied biological sciences. Psychology
Genetics
glutamic acid
Heat shock proteins
Microbiology
mutants
N2 fixation
NifH gene
Nitrogen fixation
Nitrogenase
Nitrogenation
Open reading frames
Oxygen
Paracoccus denitrificans
phenotype
Phenotypes
proteins
Rhodobacter capsulatus
Stress proteins
Tn5 mutagenesis
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Summary:Disruption of an open reading frame (ORF) of 840 bp (280 amino acids; ORF280) in an Azospirillum brasilense Tn5 mutant resulted in a pleiotrophic phenotype. Besides an enhanced N2-fixing capacity and altered expression pattern of a nifH-gusA fusion, growth on the charged polar amino acids glutamate and arginine was severely affected. ORF280, similar to previously identified ORFs present in Bradyrhizobium japonicum (ORF277), Paracoccus denitrificans (ORF278) and Rhodobacter capsulatus (ORF277), exhibits in its C-terminus a significant similarity with the recently defined family of universal stress proteins.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2000.tb08928.x