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Mutation in a D-alanine-D-alanine ligase of Azospirillum brasilense Cd results in an overproduction of exopolysaccharides and a decreased tolerance to saline stress.
Jofré, Edgardo; Fischer, Sonia; Príncipe, Analía; Castro, Marina; Ferrari, Walter; Lagares, Antonio; Mori, Gladys.
Afiliação
  • Jofré E; Departamento de Ciencias Naturales, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, Córdoba, Argentina. ejofre@exa.unrc.edu.ar
FEMS Microbiol Lett ; 290(2): 236-46, 2009 Jan.
Article em En | MEDLINE | ID: mdl-19025567
Bacteria of the genus Azospirillum are free-living nitrogen-fixing, rhizobacteria that are found in close association with plant roots, where they exert beneficial effects on plant growth and yield in many crops of agronomic importance. Unlike other bacteria, little is known about the genetics and biochemistry of exopolysaccharides in Azospirillum brasilense. In an attempt to characterize genes associated with exopolysaccharides production, we generated an A. brasilense Cd Tn5 mutant that showed exopolysaccharides overproduction, decreased tolerance to saline conditions, altered cell morphology, and increased sensitivity to detergents. Genetic characterization showed that the Tn5 was inserted within a ddlB gene encoding for a d-alanine-d-alanine ligase, and located upstream of the ftsQAZ gene cluster responsible for cell division in different bacteria. Heterologous complementation of the ddlB Tn5 mutant restored the exopolysaccharides production to wild-type levels and the ability to grow in the presence of detergents, but not the morphology and growth characteristics of the wild-type bacteria, suggesting a polar effect of Tn5 on the fts genes. This result and the construction of a nonpolar ddlB mutant provide solid evidence of the presence of transcriptional coupling between a gene associated with peptidoglycan biosynthesis and the fts genes required to control cell division.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Sintases / Polissacarídeos Bacterianos / Proteínas de Bactérias / Cloreto de Sódio / Azospirillum brasilense / Mutação País/Região como assunto: America do sul / Brasil Idioma: En Revista: FEMS Microbiol Lett Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Sintases / Polissacarídeos Bacterianos / Proteínas de Bactérias / Cloreto de Sódio / Azospirillum brasilense / Mutação País/Região como assunto: America do sul / Brasil Idioma: En Revista: FEMS Microbiol Lett Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido