NMR assignments of the GacS histidine-kinase periplasmic detection domain from Pseudomonas aeruginosa PAO1
2017
Ali-Ahmad, Ahmad | Bornet, Olivier | Fadel, Firas | Bourne, Yves | Vincent, Florence | Bordi, Christophe | Guerlesquin, Françoise | Sebban-Kreuzer, Corinne | Architecture et fonction des macromolécules biologiques (AFMB) ; Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS) | Laboratoire d'ingénierie des systèmes macromoléculaires (LISM) ; Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) | ANR-14-CE09-0005,REGALAD,Relation structure-fonction d'une famille d'histidine kinases contrôlant le mode de vie de Pseudomonas aeruginosa(2014)
International audience
Mostrar más [+] Menos [-]Inglés. Pseudomonas aeruginosa is a highly adaptable opportunistic pathogen. It can infect vulnerable patients such as those with cystic fibrosis or hospitalized in intensive care units where it is responsible for both acute and chronic infection. The switch between these infections is controlled by a complex regulatory system involving the central GacS/GacA two-component system that activates the production of two small non-coding RNAs. GacS is a histidine kinase harboring one periplasmic detection domain, two inner-membrane helices and three H1/D1/H2 cytoplasmic domains. By detecting a yet unknown signal, the GacS histidine-kinase periplasmic detection domain (GacSp) is predicted to play a key role in activating the GacS/GacA pathway. Here, we present the chemical shift assignment of 96 % of backbone atoms (HN, N, C, Ca, Cb and Ha), 88 % aliphatic hydrogen atoms and 90 % of aliphatic carbon atoms of this domain. The NMR-chemical shift data, on the basis of Talos server secondary structure predictions, reveal that GacSp consists of 3 b-strands, 3 a-helices and a major loop devoid of secondary structures.
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