Novel Tat-Dependent Protein Secretion

Braun, V; Hantke, K

doi:10.1128/JB.00058-20

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Novel Tat-Dependent Protein Secretion

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Braun, V
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Braun, V., & Hantke, K. (2020). Novel Tat-Dependent Protein Secretion. Journal of Bacteriology, 202(9): e00058-20. doi:10.1128/JB.00058-20.

Cite as: https://hdl.handle.net/21.11116/0000-000A-5E1D-E

Abstract

The transcription initiation signal elicited by the binding of ferric citrate to the outer membrane FecA protein is transmitted by the FecR protein across the cytoplasmic membrane to the FecI extracytoplasmic function (ECF) sigma factor. In this issue of Journal of Bacteriology, I. J. Passmore, J. M. Dow, F. Coll, J. Cuccui, et al. (J Bacteriol 202:e00541-19, 2020, https://doi.org/10.1128/JB.00541-19) report that the FecR sequence contains both the twin-arginine signal motif and the secretory (Sec) avoidance motif typical of proteins secreted by the twin-arginine translocation (TAT) system. The same study shows that FecR is indeed secreted by Tat and represents a new class of bitopic Tat-dependent membrane proteins.