The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria

Autores
Ensinck, Delfina; Marques Gerhardt, Edileusa Cristina; Rollan, Lara; Huergo, Luciano F.; Gramajo, Hugo Cesar; Diacovich, Lautaro
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
PII proteins are signal transduction proteins that belong to a widely distributedfamily of proteins involved in the modulation of different metabolisms in bacteria.These proteins are homotrimers carrying a flexible loop, named T-loop, whichchanges its conformation due to the recognition of diverse key metabolites,ADP, ATP, and 2-oxoglutarate. PII proteins interact with different partners toprimarily regulate a set of nitrogen pathways. In some organisms, PII proteinscan also control carbon metabolism by interacting with the biotin carboxylcarrier protein (BCCP), a key component of the acetyl-CoA carboxylase (ACC)enzyme complex, inhibiting its activity with the consequent reduction of fattyacid biosynthesis. Most bacteria contain at least two PII proteins, named GlnBand GlnK, with different regulatory roles. In mycobacteria, only one PII proteinwas identified, and the three-dimensional structure was solved, however, itsphysiological role is unknown. In this study we purified the Mycobacteriumtuberculosis (M. tb) PII protein, named GlnB, and showed that it weakly interactswith the AccA3 protein, the α subunit shared by the three different, and essential,Acyl-CoA carboxylase complexes (ACCase 4, 5, and 6) present in M. tb. A M.smegmatis deletion mutant, ΔMsPII, exhibited a growth deficiency on nitrateand nitrite as unique nitrogen sources, and accumulated nitrite in the culturesupernatant. In addition, M. tb PII protein was able to interact with the C-terminaldomain of the ammonium transporter Amt establishing the ancestral role forthis PII protein as a GlnK functioning protein.
Fil: Ensinck, Delfina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Marques Gerhardt, Edileusa Cristina. Universidade Federal do Paraná; Brasil
Fil: Rollan, Lara. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Huergo, Luciano F.. Universidade Federal do Paraná; Brasil
Fil: Gramajo, Hugo Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Diacovich, Lautaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
PII PROTEIN
MYCOBACTERIA
NITRITE ASSIMILATION
NITROGEN METABOLISM REGULATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/262878
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/262878
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteriaEnsinck, DelfinaMarques Gerhardt, Edileusa CristinaRollan, LaraHuergo, Luciano F.Gramajo, Hugo CesarDiacovich, LautaroPII PROTEINMYCOBACTERIANITRITE ASSIMILATIONNITROGEN METABOLISM REGULATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1PII proteins are signal transduction proteins that belong to a widely distributedfamily of proteins involved in the modulation of different metabolisms in bacteria.These proteins are homotrimers carrying a flexible loop, named T-loop, whichchanges its conformation due to the recognition of diverse key metabolites,ADP, ATP, and 2-oxoglutarate. PII proteins interact with different partners toprimarily regulate a set of nitrogen pathways. In some organisms, PII proteinscan also control carbon metabolism by interacting with the biotin carboxylcarrier protein (BCCP), a key component of the acetyl-CoA carboxylase (ACC)enzyme complex, inhibiting its activity with the consequent reduction of fattyacid biosynthesis. Most bacteria contain at least two PII proteins, named GlnBand GlnK, with different regulatory roles. In mycobacteria, only one PII proteinwas identified, and the three-dimensional structure was solved, however, itsphysiological role is unknown. In this study we purified the Mycobacteriumtuberculosis (M. tb) PII protein, named GlnB, and showed that it weakly interactswith the AccA3 protein, the α subunit shared by the three different, and essential,Acyl-CoA carboxylase complexes (ACCase 4, 5, and 6) present in M. tb. A M.smegmatis deletion mutant, ΔMsPII, exhibited a growth deficiency on nitrateand nitrite as unique nitrogen sources, and accumulated nitrite in the culturesupernatant. In addition, M. tb PII protein was able to interact with the C-terminaldomain of the ammonium transporter Amt establishing the ancestral role forthis PII protein as a GlnK functioning protein.Fil: Ensinck, Delfina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Marques Gerhardt, Edileusa Cristina. Universidade Federal do Paraná; BrasilFil: Rollan, Lara. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Huergo, Luciano F.. Universidade Federal do Paraná; BrasilFil: Gramajo, Hugo Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Diacovich, Lautaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFrontiers Media2024-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/262878Ensinck, Delfina; Marques Gerhardt, Edileusa Cristina; Rollan, Lara; Huergo, Luciano F.; Gramajo, Hugo Cesar; et al.; The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria; Frontiers Media; Frontiers in Microbiology; 15; 3-2024; 1-161664-302XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fmicb.2024.1366111/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2024.1366111info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:42:23Zoai:ri.conicet.gov.ar:11336/262878instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-11-12 09:42:23.498CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
title The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
spellingShingle The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
Ensinck, Delfina
PII PROTEIN
MYCOBACTERIA
NITRITE ASSIMILATION
NITROGEN METABOLISM REGULATION
title_short The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
title_full The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
title_fullStr The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
title_full_unstemmed The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
title_sort The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria
dc.creator.none.fl_str_mv Ensinck, Delfina
Marques Gerhardt, Edileusa Cristina
Rollan, Lara
Huergo, Luciano F.
Gramajo, Hugo Cesar
Diacovich, Lautaro
author Ensinck, Delfina
author_facet Ensinck, Delfina
Marques Gerhardt, Edileusa Cristina
Rollan, Lara
Huergo, Luciano F.
Gramajo, Hugo Cesar
Diacovich, Lautaro
author_role author
author2 Marques Gerhardt, Edileusa Cristina
Rollan, Lara
Huergo, Luciano F.
Gramajo, Hugo Cesar
Diacovich, Lautaro
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv PII PROTEIN
MYCOBACTERIA
NITRITE ASSIMILATION
NITROGEN METABOLISM REGULATION
topic PII PROTEIN
MYCOBACTERIA
NITRITE ASSIMILATION
NITROGEN METABOLISM REGULATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv PII proteins are signal transduction proteins that belong to a widely distributedfamily of proteins involved in the modulation of different metabolisms in bacteria.These proteins are homotrimers carrying a flexible loop, named T-loop, whichchanges its conformation due to the recognition of diverse key metabolites,ADP, ATP, and 2-oxoglutarate. PII proteins interact with different partners toprimarily regulate a set of nitrogen pathways. In some organisms, PII proteinscan also control carbon metabolism by interacting with the biotin carboxylcarrier protein (BCCP), a key component of the acetyl-CoA carboxylase (ACC)enzyme complex, inhibiting its activity with the consequent reduction of fattyacid biosynthesis. Most bacteria contain at least two PII proteins, named GlnBand GlnK, with different regulatory roles. In mycobacteria, only one PII proteinwas identified, and the three-dimensional structure was solved, however, itsphysiological role is unknown. In this study we purified the Mycobacteriumtuberculosis (M. tb) PII protein, named GlnB, and showed that it weakly interactswith the AccA3 protein, the α subunit shared by the three different, and essential,Acyl-CoA carboxylase complexes (ACCase 4, 5, and 6) present in M. tb. A M.smegmatis deletion mutant, ΔMsPII, exhibited a growth deficiency on nitrateand nitrite as unique nitrogen sources, and accumulated nitrite in the culturesupernatant. In addition, M. tb PII protein was able to interact with the C-terminaldomain of the ammonium transporter Amt establishing the ancestral role forthis PII protein as a GlnK functioning protein.
Fil: Ensinck, Delfina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Marques Gerhardt, Edileusa Cristina. Universidade Federal do Paraná; Brasil
Fil: Rollan, Lara. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Huergo, Luciano F.. Universidade Federal do Paraná; Brasil
Fil: Gramajo, Hugo Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Diacovich, Lautaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description PII proteins are signal transduction proteins that belong to a widely distributedfamily of proteins involved in the modulation of different metabolisms in bacteria.These proteins are homotrimers carrying a flexible loop, named T-loop, whichchanges its conformation due to the recognition of diverse key metabolites,ADP, ATP, and 2-oxoglutarate. PII proteins interact with different partners toprimarily regulate a set of nitrogen pathways. In some organisms, PII proteinscan also control carbon metabolism by interacting with the biotin carboxylcarrier protein (BCCP), a key component of the acetyl-CoA carboxylase (ACC)enzyme complex, inhibiting its activity with the consequent reduction of fattyacid biosynthesis. Most bacteria contain at least two PII proteins, named GlnBand GlnK, with different regulatory roles. In mycobacteria, only one PII proteinwas identified, and the three-dimensional structure was solved, however, itsphysiological role is unknown. In this study we purified the Mycobacteriumtuberculosis (M. tb) PII protein, named GlnB, and showed that it weakly interactswith the AccA3 protein, the α subunit shared by the three different, and essential,Acyl-CoA carboxylase complexes (ACCase 4, 5, and 6) present in M. tb. A M.smegmatis deletion mutant, ΔMsPII, exhibited a growth deficiency on nitrateand nitrite as unique nitrogen sources, and accumulated nitrite in the culturesupernatant. In addition, M. tb PII protein was able to interact with the C-terminaldomain of the ammonium transporter Amt establishing the ancestral role forthis PII protein as a GlnK functioning protein.
publishDate 2024
dc.date.none.fl_str_mv 2024-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/262878
Ensinck, Delfina; Marques Gerhardt, Edileusa Cristina; Rollan, Lara; Huergo, Luciano F.; Gramajo, Hugo Cesar; et al.; The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria; Frontiers Media; Frontiers in Microbiology; 15; 3-2024; 1-16
1664-302X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/262878
identifier_str_mv Ensinck, Delfina; Marques Gerhardt, Edileusa Cristina; Rollan, Lara; Huergo, Luciano F.; Gramajo, Hugo Cesar; et al.; The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria; Frontiers Media; Frontiers in Microbiology; 15; 3-2024; 1-16
1664-302X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fmicb.2024.1366111/full
info:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2024.1366111
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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