Luíza M. Araújo

TL;DR: The genome sequence revealed that H. seropedicae is a highly versatile microorganism with capacity to metabolize a wide range of carbon and nitrogen sources and with possession of four distinct terminal oxidases, suggesting a high potential to interact with host plants.

TL;DR: In this study, in vitro complex formation between the AmtB and PII proteins (GlnB and GlnZ) and the nitrogenase regulatory enzyme DraG, which was stimulated by ADP defines a new regulatory role for Amt proteins in Prokaryotes.

TL;DR: The results show that the GlnB protein is required for transcription activation by Azospirillum brasilense NifA and it cannot be replaced by GlnZ or GlnK.

TL;DR: The results suggest that the differences in the uridylylation pattern of GlnB and GlnZ might be important for fine-tuning of the signaling pathway of cellular nitrogen status in A. brasilense.

TL;DR: The P(II) proteins comprise a family of widely distributed signal transduction proteins that integrate the signals of cellular nitrogen, carbon and energy status, and then regulate, by protein-protein interaction, the activity of a variety of target proteins including enzymes, transcriptional regulators and membrane transporters.