Journal
MICROBIOLOGICAL RESEARCH
Volume 166, Issue 8, Pages 595-605Publisher
ELSEVIER GMBH
DOI: 10.1016/j.micres.2010.11.007
Keywords
cDNA-AFLP; Chemotaxis; Encystment; Nitrogen fixation; Azospirillum brosilense
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Funding
- National Nature Science Foundation of China [30470028]
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Our previous study indicated org35 was involved in chemotaxis and interacted with nitrogen fixation transcriptional activator NifA via PAS domain. In order to reveal the role of org35 in nitrogen regulation, the downstream target genes of org35 were identified. We here report differentially expressed genes in org35 mutants comparing with wild type Sp7 by means of cDNA-AFLP. Four up-regulated transcript-derived fragments (TDFs) homologues of chemotaxis transduction proteins were found, including CheW, methyl-accepting chemotaxis protein and response regulator CheY-like receiver. Three distinct TDFs (AB46, AB58 and AB63) were similar to PHB de-polymerase C-terminus, cell shape-determining protein and flagellin domain protein. And 11 TDFs showed similarities with signal transduction proteins, including homologous protein of the nitrogen regulation protein NtrY and nitrate/nitrite response regulator protein NarL. These data suggested that the Azospirillum brasilense org35 was a multi-effecter and involved in chemotaxis, cyst development and regulation of nitrogen fixation. (C) 2010 Elsevier GmbH. All rights reserved.
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