Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase.

Gallego-Parrilla, José Jesús; Severi, Emmanuele; Chandra, Govind; Palmer, Tracy

Gallego-Parrilla, José Jesús; Severi, Emmanuele; Chandra, Govind; Palmer, Tracy.

Afiliación

Gallego-Parrilla JJ; Microbes in Health and Disease Theme, Newcastle University Biosciences Institute, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Severi E; Microbes in Health and Disease Theme, Newcastle University Biosciences Institute, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Chandra G; John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
Palmer T; Microbes in Health and Disease Theme, Newcastle University Biosciences Institute, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.

Microbiology (Reading) ; 170(2)2024 02.

Article en En | MEDLINE | ID: mdl-38363712

ABSTRACT

ABSTRACT

The twin-arginine protein transport (Tat) system exports folded proteins across the cytoplasmic membranes of prokaryotes and the energy transducing-membranes of plant thylakoids and mitochondria. Proteins are targeted to the Tat machinery by N-terminal signal peptides with a conserved twin-arginine motif, and some substrates are exported as heterodimers where the signal peptide is present on one of the partner proteins. A subset of Tat substrates is found in the membrane. Tat-dependent membrane proteins usually have large globular domains and a single transmembrane helix present at the N- or C-terminus. Five Tat substrates that have C-terminal transmembrane helices have previously been characterized in the model bacterium Escherichia coli. Each of these is an iron-sulfur cluster-containing protein involved in electron transfer from hydrogen or formate. Here we have undertaken a bioinformatic search to identify further tail-anchored Tat substrates encoded in bacterial genomes. Our analysis has revealed additional tail-anchored iron-sulfur proteins associated in modules with either a b-type cytochrome or a quinol oxidase. We also identified further candidate tail-anchored Tat substrates, particularly among members of the actinobacterial phylum, that are not predicted to contain cofactors. Using reporter assays, we show experimentally that six of these have both N-terminal Tat signal peptides and C-terminal transmembrane helices. The newly identified proteins include a carboxypeptidase and a predicted protease, and four sortase substrates for which membrane integration is a prerequisite for covalent attachment to the cell wall.

Asunto(s)

Proteínas de Escherichia coli; Proteínas de la Membrana; Proteínas de la Membrana/genética; Proteínas de la Membrana/metabolismo; Proteínas de Transporte de Membrana/metabolismo; Proteínas de Escherichia coli/metabolismo; Transporte de Proteínas; Arginina/metabolismo; Proteínas Portadoras/metabolismo; Señales de Clasificación de Proteína; Escherichia coli/genética; Escherichia coli/metabolismo; Proteínas Bacterianas/genética; Proteínas Bacterianas/metabolismo

Palabras clave

Tat pathway; bioinformatics; membrane protein; tail-anchored; twin-arginine signal peptide

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Escherichia coli / Proteínas de la Membrana Idioma: En Revista: Microbiology (Reading) Asunto de la revista: MICROBIOLOGIA Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido

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