Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation

Autores
Viale, A.A.; Wider, E.A.; Del C. Batlle, A.M.
Año de publicación
1987
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthesis abruptly halted leading to diminished steady-state specific Bchl content. When flushing oxygen was interrupted, enzymic activity increased, whether chloramphenicol was present or not in the medium; if the protein synthesis inhibitor was added when oxygenation started, ALA-S declined in the same fashion as in its absence, but thereafter reactivation of the enzyme was lower than before. Succinyl-CoA-synthetase and ALA-dehydratase activities were also measured under the conditions described, and no changes at all have been observed. The existence of different forms of ALA-S in R. palustris depending on growth conditions is postulated along with the formation of low molecular weight factors which can modulate ALA-S activity by binding to the enzyme; a widespread mechanism in the adaptation of micro-organisms to changes in environment. It is also proposed that this particular regulatory phenomenon, could be referred to as a switch off/on mechanism controlling ALA-S activity in R. palustris. © 1987.
Fil:Viale, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Int. J. Biochem. 1987;19(4):379-383
Materia
5 aminolevulinate synthase
bacteriochlorophyll
chloramphenicol
porphyrin
adaptation
article
biosynthesis
enzymology
homeostasis
metabolism
oxidation reduction reaction
Rhodopseudomonas
5-Aminolevulinate Synthetase
Adaptation, Physiological
Bacteriochlorophylls
Chloramphenicol
Homeostasis
Oxidation-Reduction
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_0020711X_v19_n4_p379_Viale

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oai_identifier_str paperaa:paper_0020711X_v19_n4_p379_Viale
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulationViale, A.A.Wider, E.A.Del C. Batlle, A.M.5 aminolevulinate synthasebacteriochlorophyllchloramphenicolporphyrinadaptationarticlebiosynthesisenzymologyhomeostasismetabolismoxidation reduction reactionRhodopseudomonas5-Aminolevulinate SynthetaseAdaptation, PhysiologicalBacteriochlorophyllsChloramphenicolHomeostasisOxidation-ReductionPorphyrinsRhodopseudomonasSupport, Non-U.S. Gov'tThe high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthesis abruptly halted leading to diminished steady-state specific Bchl content. When flushing oxygen was interrupted, enzymic activity increased, whether chloramphenicol was present or not in the medium; if the protein synthesis inhibitor was added when oxygenation started, ALA-S declined in the same fashion as in its absence, but thereafter reactivation of the enzyme was lower than before. Succinyl-CoA-synthetase and ALA-dehydratase activities were also measured under the conditions described, and no changes at all have been observed. The existence of different forms of ALA-S in R. palustris depending on growth conditions is postulated along with the formation of low molecular weight factors which can modulate ALA-S activity by binding to the enzyme; a widespread mechanism in the adaptation of micro-organisms to changes in environment. It is also proposed that this particular regulatory phenomenon, could be referred to as a switch off/on mechanism controlling ALA-S activity in R. palustris. © 1987.Fil:Viale, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1987info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_VialeInt. J. Biochem. 1987;19(4):379-383reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:00Zpaperaa:paper_0020711X_v19_n4_p379_VialeInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:01.805Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
spellingShingle Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
Viale, A.A.
5 aminolevulinate synthase
bacteriochlorophyll
chloramphenicol
porphyrin
adaptation
article
biosynthesis
enzymology
homeostasis
metabolism
oxidation reduction reaction
Rhodopseudomonas
5-Aminolevulinate Synthetase
Adaptation, Physiological
Bacteriochlorophylls
Chloramphenicol
Homeostasis
Oxidation-Reduction
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
title_short Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_full Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_fullStr Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_full_unstemmed Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_sort Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
dc.creator.none.fl_str_mv Viale, A.A.
Wider, E.A.
Del C. Batlle, A.M.
author Viale, A.A.
author_facet Viale, A.A.
Wider, E.A.
Del C. Batlle, A.M.
author_role author
author2 Wider, E.A.
Del C. Batlle, A.M.
author2_role author
author
dc.subject.none.fl_str_mv 5 aminolevulinate synthase
bacteriochlorophyll
chloramphenicol
porphyrin
adaptation
article
biosynthesis
enzymology
homeostasis
metabolism
oxidation reduction reaction
Rhodopseudomonas
5-Aminolevulinate Synthetase
Adaptation, Physiological
Bacteriochlorophylls
Chloramphenicol
Homeostasis
Oxidation-Reduction
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
topic 5 aminolevulinate synthase
bacteriochlorophyll
chloramphenicol
porphyrin
adaptation
article
biosynthesis
enzymology
homeostasis
metabolism
oxidation reduction reaction
Rhodopseudomonas
5-Aminolevulinate Synthetase
Adaptation, Physiological
Bacteriochlorophylls
Chloramphenicol
Homeostasis
Oxidation-Reduction
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
dc.description.none.fl_txt_mv The high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthesis abruptly halted leading to diminished steady-state specific Bchl content. When flushing oxygen was interrupted, enzymic activity increased, whether chloramphenicol was present or not in the medium; if the protein synthesis inhibitor was added when oxygenation started, ALA-S declined in the same fashion as in its absence, but thereafter reactivation of the enzyme was lower than before. Succinyl-CoA-synthetase and ALA-dehydratase activities were also measured under the conditions described, and no changes at all have been observed. The existence of different forms of ALA-S in R. palustris depending on growth conditions is postulated along with the formation of low molecular weight factors which can modulate ALA-S activity by binding to the enzyme; a widespread mechanism in the adaptation of micro-organisms to changes in environment. It is also proposed that this particular regulatory phenomenon, could be referred to as a switch off/on mechanism controlling ALA-S activity in R. palustris. © 1987.
Fil:Viale, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description The high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthesis abruptly halted leading to diminished steady-state specific Bchl content. When flushing oxygen was interrupted, enzymic activity increased, whether chloramphenicol was present or not in the medium; if the protein synthesis inhibitor was added when oxygenation started, ALA-S declined in the same fashion as in its absence, but thereafter reactivation of the enzyme was lower than before. Succinyl-CoA-synthetase and ALA-dehydratase activities were also measured under the conditions described, and no changes at all have been observed. The existence of different forms of ALA-S in R. palustris depending on growth conditions is postulated along with the formation of low molecular weight factors which can modulate ALA-S activity by binding to the enzyme; a widespread mechanism in the adaptation of micro-organisms to changes in environment. It is also proposed that this particular regulatory phenomenon, could be referred to as a switch off/on mechanism controlling ALA-S activity in R. palustris. © 1987.
publishDate 1987
dc.date.none.fl_str_mv 1987
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/20.500.12110/paper_0020711X_v19_n4_p379_Viale
url http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Int. J. Biochem. 1987;19(4):379-383
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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