TY - JOUR
T1 - Regulation of (p)ppGpp hydrolysis by a conserved archetypal regulatory domain
AU - Ronneau, Séverin
AU - Caballero-Montes, Julien
AU - Coppine, Jérôme
AU - Mayard, Aurélie
AU - Garcia-Pino, Abel
AU - Hallez, Régis
N1 - Funding Information:
Fonds de la Recherche Scientifique - FNRS (F.R.S.-FNRS) [CDR J.0169.16 to R.H.]; [EQP U.N043.17F; WELBIO CR-2017S-03; PDR T.0066.18 to A.G-P.]; Programme ‘Actions de Recherche Concertée’ 2016–2021 from the ULB and the Fonds d’Encouragement à la Recherche ULB (FER-ULB to A.G-P.); FRIA (Fund for Research Training in Industry and Agriculture) fellowships from the F.R.S.-FNRS to S.R. and J.C-M. R.H. is a Research Associate of the F.R.S.-FNRS. Funding for open access charge: University of Namur. Conflict of interest statement. None declared.
Funding Information:
Fonds de la Recherche Scientifique - FNRS (F.R.S.-FNRS) [CDR J.0169.16 to R.H.]; [EQP U.N043.17F; WELBIO CR-2017S-03; PDR T.0066.18 to A.G-P.]; Programme 'Actions de Recherche Concertée' 2016-2021 from the ULB and the Fonds d'Encouragement à la Recherche ULB (FER-ULB to A.G-P.); FRIA (Fund for Research Training in Industry and Agriculture) fellowships from the F.R.S.- FNRS to S.R. and J.C-M. R.H. is a Research Associate of the F.R.S.-FNRS. Funding for open access charge: University of Namur.
Publisher Copyright:
© The Author(s) 2018.
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2019/1/25
Y1 - 2019/1/25
N2 - Sensory and regulatory domains allow bacteria to adequately respond to environmental changes. The regulatory ACT (Aspartokinase, Chorismate mutase and TyrA) domains are mainly found in metabolic-related proteins as well as in long (p)ppGpp synthetase/hydrolase enzymes. Here, we investigate the functional role of the ACT domain of SpoT, the only (p)ppGpp synthetase/hydrolase of Caulobacter crescentus. We show that SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. In addition, our in vivo and in vitro data show that the phosphorylated version of EIIANtr (EIIANtr∼P) interacts directly with the ACT and inhibits the hydrolase activity of SpoT. Finally, we highlight the conservation of the ACT-dependent interaction between EIIANtr∼P and SpoT/Rel along with the phosphotransferase system (PTSNtr)-dependent regulation of (p)ppGpp accumulation upon nitrogen starvation in Sinorhizobium meliloti, a plant-associated α-proteobacterium. Thus, this work suggests that α-proteobacteria might have inherited from a common ancestor, a PTSNtr dedicated to modulate (p)ppGpp levels in response to nitrogen availability.
AB - Sensory and regulatory domains allow bacteria to adequately respond to environmental changes. The regulatory ACT (Aspartokinase, Chorismate mutase and TyrA) domains are mainly found in metabolic-related proteins as well as in long (p)ppGpp synthetase/hydrolase enzymes. Here, we investigate the functional role of the ACT domain of SpoT, the only (p)ppGpp synthetase/hydrolase of Caulobacter crescentus. We show that SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. In addition, our in vivo and in vitro data show that the phosphorylated version of EIIANtr (EIIANtr∼P) interacts directly with the ACT and inhibits the hydrolase activity of SpoT. Finally, we highlight the conservation of the ACT-dependent interaction between EIIANtr∼P and SpoT/Rel along with the phosphotransferase system (PTSNtr)-dependent regulation of (p)ppGpp accumulation upon nitrogen starvation in Sinorhizobium meliloti, a plant-associated α-proteobacterium. Thus, this work suggests that α-proteobacteria might have inherited from a common ancestor, a PTSNtr dedicated to modulate (p)ppGpp levels in response to nitrogen availability.
UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85060607525&origin=resultslist&sort=plf-f&src=s&sid=64dffd42541a00c8a515072557292d10&sot=autdocs&sdt=autdocs&sl=17&s=AU-ID%286603142172%29&relpos=0&citeCnt=0&searchTerm=
U2 - 10.1093/nar/gky1201
DO - 10.1093/nar/gky1201
M3 - Article
SN - 0305-1048
VL - 47
SP - 843
EP - 854
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 2
ER -
