Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA
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Título: | Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA |
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Autor/es: | Jerez García, Carmen | Salinas, Paloma | Llop Estevez, Antonio | Cantos, Raquel | Espinosa, Javier | Labella, Jose I. | Contreras, Asunción |
Grupo/s de investigación o GITE: | Transducción de Señales en Bacterias |
Centro, Departamento o Servicio: | Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología |
Palabras clave: | Protein interaction | PII | Synechococcus elongatus | Bacterial two hybrid | Phenotypic analysis | Confocal microscopy | Nitrogen regulation network |
Área/s de conocimiento: | Genética |
Fecha de publicación: | 9-dic-2021 |
Editor: | Frontiers Media |
Cita bibliográfica: | Jerez C, Salinas P, Llop A, Cantos R, Espinosa J, Labella JI and Contreras A (2021) Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA. Front. Microbiol. 12:781760. doi: 10.3389/fmicb.2021.781760 |
Resumen: | Cyanobacteria, phototrophic organisms performing oxygenic photosynthesis, must adapt their metabolic processes to important environmental challenges, like those imposed by the succession of days and nights. Not surprisingly, certain regulatory proteins are found exclusively in this phylum. One of these unique proteins, PipX, provides a mechanistic link between signals of carbon/nitrogen and of energy, transduced by the signaling protein PII, and the control of gene expression by the global nitrogen regulator NtcA. PII, required for cell survival unless PipX is inactivated or downregulated, functions by protein–protein interactions with transcriptional regulators, transporters, and enzymes. PipX also functions by protein–protein interactions, and previous studies suggested the existence of additional interacting partners or included it into a relatively robust six-node synteny network with proteins apparently unrelated to the nitrogen regulation system. To investigate additional functions of PipX while providing a proof of concept for the recently developed cyanobacterial linkage network, here we analyzed the physical and regulatory interactions between PipX and an intriguing component of the PipX synteny network, the essential ribosome assembly GTPase EngA. The results provide additional insights into the functions of cyanobacterial EngA and of PipX, showing that PipX interacts with the GD1 domain of EngA in a guanosine diphosphate-dependent manner and interferes with EngA functions in Synechococcus elongatus at a low temperature, an environmentally relevant context. Therefore, this work expands the PipX interaction network and establishes a possible connection between nitrogen regulation and the translation machinery. We discuss a regulatory model integrating previous information on PII–PipX with the results presented in this work. |
Patrocinador/es: | This work was supported by grant PID2020-118816GB-I00 to AC from the Spanish Government (MICINN), grant AICO/2020/057 to JE from the Conselleria d’Innovació, Universitats, Ciència i Societat Digital of the Generalitat Valenciana, and grants VIGROB-126/19, VIGROB20-126, GRE20-04-C, and UAUSTI19-06 to AC from the University of Alicante. CJ was the recipient of a Ph.D. fellowship (ACIF/2019/045) from Conselleria d’Innovació, Universitats, Ciència i Societat Digital of the Generalitat Valenciana. |
URI: | http://hdl.handle.net/10045/120074 |
ISSN: | 1664-302X |
DOI: | 10.3389/fmicb.2021.781760 |
Idioma: | eng |
Tipo: | info:eu-repo/semantics/article |
Derechos: | © 2021 Jerez, Salinas, Llop, Cantos, Espinosa, Labella and Contreras. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
Revisión científica: | si |
Versión del editor: | https://doi.org/10.3389/fmicb.2021.781760 |
Aparece en las colecciones: | INV - TSB - Artículos de Revistas |
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