The protein-protein interaction network of the Escherichia coli EIIA Ntr regulatory protein reveals a role in cell motility and metabolic control.

Autor: Gravina F; Departamento de Bioquímica e Biologia Molecular, UFPR, Curitiba, PR, Brazil., Degaut FL; Departamento de Bioquímica e Biologia Molecular, UFPR, Curitiba, PR, Brazil., Gerhardt ECM; Departamento de Bioquímica e Biologia Molecular, UFPR, Curitiba, PR, Brazil., Pedrosa FO; Departamento de Bioquímica e Biologia Molecular, UFPR, Curitiba, PR, Brazil., Souza EM; Departamento de Bioquímica e Biologia Molecular, UFPR, Curitiba, PR, Brazil., Antônio de Souza G; Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil., Huergo LF; Departamento de Bioquímica e Biologia Molecular, UFPR, Curitiba, PR, Brazil; Setor Litoral, UFPR, Matinhos, PR, Brazil. Electronic address: huergo@ufpr.br.
Jazyk: angličtina
Zdroj: Research in microbiology [Res Microbiol] 2021 Nov-Dec; Vol. 172 (7-8), pp. 103882. Date of Electronic Publication: 2021 Sep 23.
DOI: 10.1016/j.resmic.2021.103882
Abstrakt: The nitrogen-related PTS Ntr system, present in many Proteobacteria including Escherichia coli, acts as a phosphorelay cascade composed of the EI Ntr , NPr and EIIA Ntr proteins. Phosphotransfer initiates with phosphoenolpyruvate-dependent EI Ntr autophosphorylation, the phosphoryl group is then transferred to NPr and finally to a conserved histidine residue on EIIA Ntr . The reporter metabolites l-glutamine and 2-oxoglutarate reciprocally regulate EI Ntr autophosphorylation (Lee et al., 2013) and consequently the phosphorylation status of the PTS Ntr components is controlled by the availability of nitrogen and carbon. The final phosphate acceptor, EIIA Ntr , regulates a range of cellular process by acting as the central hub of a complex protein-protein interaction network. Contact between EIIA Ntr and its target proteins is usually regulated by the EIIA Ntr phosphorylation status. In this study we performed ligand fishing assays coupled to label-free quantitative proteomics to examine the protein-protein interaction network of E. coli EIIA Ntr and a phosphomimic variant of the protein. The ligand fishing data, along with phenotypic analysis, indicated that EIIA Ntr interacts with proteins related to chemotaxis and thereby regulates cell motility. Important metabolic enzymes were also identified as potential EIIA Ntr binding partners.
Competing Interests: Declaration of competing interest Authors have no conflict of interest to declare.
(Copyright © 2021 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.)
Databáze: MEDLINE
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