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

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) synthes...

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Autores principales: Viale, Alberto Américo, Batlle, Alcira María del Carmen
Publicado: 1987
Materias:
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
Support, Non-U.S. Gov't
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n4_p379_Viale
http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_0020711X_v19_n4_p379_Viale
record_format dspace
spelling paper:paper_0020711X_v19_n4_p379_Viale2023-06-08T14:41:09Z Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation Viale, Alberto Américo Batlle, Alcira María del Carmen 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 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. 1987 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n4_p379_Viale http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
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
spellingShingle 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
Viale, Alberto Américo
Batlle, Alcira María del Carmen
Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
topic_facet 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
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.
author Viale, Alberto Américo
Batlle, Alcira María del Carmen
author_facet Viale, Alberto Américo
Batlle, Alcira María del Carmen
author_sort Viale, Alberto Américo
title Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
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
publishDate 1987
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n4_p379_Viale
http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
work_keys_str_mv AT vialealbertoamerico porphyrinbiosynthesisinrhodopseudomonaspalustrisxiidaminolevulinatesynthetaseswitchoffonregulation
AT batllealciramariadelcarmen porphyrinbiosynthesisinrhodopseudomonaspalustrisxiidaminolevulinatesynthetaseswitchoffonregulation
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