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Detalle de: Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism

Title Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism
Abstract

Iron is essential for nearly all living organisms due to its role in metabolic processes and as a cofactor for many enzymes. The FecRI signal transduction pathway regulates citrate-mediated iron import in many Gram-negative bacteria, including Escherichia coli . The interactions of FecR with the outer membrane protein FecA and cytoplasmic anti-sigma factor FecI have been extensively studied. However, the mechanism by which FecR inserts into the membrane has not previously been reported. In this study, we demonstrate that the targeting of FecR to the cytoplasmic membrane is dependent on the Tat system. As such, FecR represents a new class of bitopic Tat-dependent membrane proteins with an internal twin-arginine signal sequence.

Apa Reference Passmore, I. J., Dow, J. M., Coll, F., Cuccui, J., Palmer, T., & Wren, B. W. (2020). Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism. Journal of Bacteriology, 202(9). 10.1128/jb.00541-19
Doi 10.1128/jb.00541-19
Publication Date 9 Apr 2020
Publication Type Article
Researcher Francesc Coll I Cerezo
Ontology Model organisms
Research Groups Applied Microbial Genomics
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