Heme inhibits the activity of a c-di-GMP phosphodiesterase in Vibrio cholerae.
Biochem Biophys Res Commun
; 529(4): 1112-1116, 2020 09 03.
Article
em En
| MEDLINE
| ID: mdl-32819573
ABSTRACT
Heme, a complex of iron and protoporphyrin IX, plays an essential role in numerous biological processes including oxygen transport, oxygen storage, and electron transfer. The role of heme as a prosthetic group in bacterial hemoprotein gas sensors, which utilize heme as a cofactor for the binding of diatomic gas molecules, has been well studied. Less well known is the role of protein sensors of heme. In this report, we characterize the heme binding properties of a phosphodiesterase, CdpA, from Vibrio cholerae. We demonstrate that the N-terminal domain of CdpA is a NosP domain capable of heme binding, which consequently inhibits the c-di-GMP hydrolysis activity of the C-terminal phosphodiesterase domain. Further evidence for CdpA as a heme responsive sensor is supported by a relatively fast rate of heme dissociation. This study provides insight into an emerging class of heme-responsive sensor proteins.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Inibidores de Fosfodiesterase
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Proteínas de Bactérias
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Vibrio cholerae
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Diester Fosfórico Hidrolases
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Heme
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article