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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v19_n4_p379_Viale
Ver los metadatos del registro completo
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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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1844618737326489600 |
score |
13.070432 |