Role of PII proteins in nitrogen fixation control of <it>Herbaspirillum seropedicae </it>strain SmR1

• Main Authors: Steffens Maria BR, Pedrosa Fabio O, Rigo Liu U, Souza Emanuel M, Bonatto Ana C, Monteiro Rose A, Noindorf Lilian, Chubatsu Leda S
• Format: Article
• Language: English
• Published: BMC 2011-01-01
• Series: BMC Microbiology
• Online Access: http://www.biomedcentral.com/1471-2180/11/8

<p>Abstract</p> <p>Background</p> <p>The PII protein family comprises homotrimeric proteins which act as transducers of the cellular nitrogen and carbon status in prokaryotes and plants. In <it>Herbaspirillum seropedicae</it>, two PII-like proteins (GlnB and GlnK), encoded by the genes <it>glnB </it>and <it>glnK</it>, were identified. The <it>glnB </it>gene is monocistronic and its expression is constitutive, while <it>glnK </it>is located in the <it>nlmAglnKamtB </it>operon and is expressed under nitrogen-limiting conditions.</p> <p>Results</p> <p>In order to determine the involvement of the <it>H. seropedicae glnB </it>and <it>glnK </it>gene products in nitrogen fixation, a series of mutant strains were constructed and characterized. The <it>glnK^-</it>mutants were deficient in nitrogen fixation and they were complemented by plasmids expressing the GlnK protein or an N-truncated form of NifA. The nitrogenase post-translational control by ammonium was studied and the results showed that the <it>glnK </it>mutant is partially defective in nitrogenase inactivation upon addition of ammonium while the <it>glnB </it>mutant has a wild-type phenotype.</p> <p>Conclusions</p> <p>Our results indicate that GlnK is mainly responsible for NifA activity regulation and ammonium-dependent post-translational regulation of nitrogenase in <it>H. seropedicae</it>.</p>