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RelA/SpoT Homologs enzymes in bacteria: structural and molecular characterization of their activity and interactions with molecular partners

par Caballero Montes, Julien
Président du jury Vanhamme, Luc
Promoteur Garcia-Pino, Abel
Publication Non publié, 2022-07-11

Thèse de doctorat

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Résumé :

RelA/SpoT Homologs (RSH) enzymes control the bacterial stringent response through the synthesis and hydrolysis of the alarmone (p)ppGpp. Current biochemical and structural data is not sufficient to correctly understand RSH enzymatic activity as well as their regulation and interaction with molecular partners. This doctoral thesis has demonstrated the implication of Rel ACT domain in the regulation of its enzymatic activity and its interaction with the EIIANtr protein in Caulobacter crescentus. In addition, it has also confirmed the presence of a dedicated (p)ppGpp allosteric binding site in the catalytic domain of Rel in Bacillus subtilis and characterized the regulation of the latter’s activity during potassium starvation, notably by the resolution of the crystallographic structure of Rel complexed with the DarB protein. Through the discovery of these novel results, this thesis deepens the fundamental workings of RSH activity regulation.