A mammalian mitochondrial drug receptor functions as a bacterial "oxygen" sensor.
Proc Natl Acad Sci U S A
; 94(10): 5101-6, 1997 May 13.
Article
en En
| MEDLINE
| ID: mdl-9144197
The rat mitochondrial outer membrane-localized benzodiazepine receptor (MBR) was expressed in wild-type and TspO- (tryptophan-rich sensory protein) strains of the facultative photoheterotroph, Rhodobacter sphaeroides 2.4.1, and was shown to retain its structure within the bacterial outer membrane as assayed by its binding properties with a variety of MBR ligands. Functionally, it was able to substitute for TspO by negatively regulating the expression of photosynthesis genes in response to oxygen. This effect was reversed pharmacologically with the MBR ligand PK11195. These results suggest a close evolutionary and functional relationship between the bacterial TspO and the MBR. This relationship provides further support for the origin of the mammalian mitochondrion from a "photosynthetic" precursor. Finally, these findings provide novel insights into the physiological role that has been obscure for the MBR in situ.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oxígeno
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Proteínas Bacterianas
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Rhodobacter sphaeroides
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Receptores de GABA-A
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Membranas Intracelulares
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Proteínas de la Membrana
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Mitocondrias
Límite:
Animals
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos