Skip to Main content Skip to Navigation
Journal articles

$Rhodobacter\ sphaeroides$ methionine sulfoxide reductase P reduces $R$ ‑ and $S$ ‑diastereomers of methionine sulfoxide from a broad‑spectrum of protein substrates

Lionel Tarrago 1, 2, * Sandrine Grosse 1, 2 Marina Siponen 1, 2 David Lemaire 1, 3 Béatrice Alonso 1, 2 Guylaine Miotello 4 Jean Armengaud 4 Pascal Arnoux 1, 2 David Pignol 1, 2 Monique Sabaty 1, 2, *
* Corresponding author
2 MEM - Microbiologie Environnementale et Moléculaire
BIAM - Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) : DRF/BIAM
3 IPM - Interactions Protéine Métal
BIAM - Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) : DRF/BIAM
4 LI2D - Laboratoire Innovations technologiques pour la Détection et le Diagnostic
SPI - Service de Pharmacologie et Immunoanalyse : DRF/JOLIOT
Abstract : Methionine (Met) is prone to oxidation and can be converted to Met sulfoxide (MetO), which exists as $R$- and $S$-diastereomers. MetO can be reduced back to Met by the ubiquitous methionine sulfoxide reductase (Msr) enzymes. Canonical MsrA and MsrB were shown to be absolutely stereospecific for the reduction of S ‑ and R‑ diastereomer, respectively. Recently, a new enzymatic system, MsrQ/MsrP which is conserved in all gram‑negative bacteria, was identified as a key actor in the reduction of oxidized periplasmic proteins. The haem‑binding membrane protein MsrQ transmits reducing power from the electron transport chains to the molybdoenzyme MsrP, which acts as a protein‑MetO reductase. The MsrQ/MsrP function was well established genetically, but the identity and biochemical properties of MsrP substrates remain unknown. In this work, using the purified MsrP enzyme from the photosynthetic bacteria $Rhodobacter\ sphaeroides$ as a model, we show that it can reduce a broad spectrum of protein substrates. The most efficiently reduced MetO are found in clusters of amino acid sequences devoid of threonine and proline on the C‑terminal side. Moreover, $R.\ sphaeroides$ MsrP lacks stereospecificity as it can reduce both R‑ and S‑ diastereomers of MetO, similarly to its $Escherichia\ coli$ homolog, and preferentially acts on unfolded oxidized proteins. Overall, these results provide important insights into the function of a bacterial envelop protecting system, which should help understand how bacteria cope in harmful environments.
Complete list of metadatas

https://hal-cea.archives-ouvertes.fr/cea-01936753
Contributor : Véronique Lamare <>
Submitted on : Thursday, December 13, 2018 - 2:52:23 PM
Last modification on : Thursday, November 26, 2020 - 3:08:51 AM

Identifiers

Collections

Citation

Lionel Tarrago, Sandrine Grosse, Marina Siponen, David Lemaire, Béatrice Alonso, et al.. $Rhodobacter\ sphaeroides$ methionine sulfoxide reductase P reduces $R$ ‑ and $S$ ‑diastereomers of methionine sulfoxide from a broad‑spectrum of protein substrates. Biochemical Journal, Portland Press, 2018, 475 (23), pp.3779-3795. ⟨10.1042/BCJ20180706⟩. ⟨cea-01936753⟩

Share

Metrics

Record views

153

Files downloads

302