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Inner Membrane Translocases and Insertases

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Bacterial Cell Walls and Membranes

Part of the book series: Subcellular Biochemistry ((SCBI,volume 92))

Abstract

The inner membrane of Gram-negative bacteria is a ~6 nm thick phospholipid bilayer. It forms a semi-permeable barrier between the cytoplasm and periplasm allowing only regulated export and import of ions, sugar polymers, DNA and proteins. Inner membrane proteins, embedded via hydrophobic transmembrane α-helices, play an essential role in this regulated trafficking: they mediate insertion into the membrane (insertases) or complete crossing of the membrane (translocases) or both. The Gram-negative inner membrane is equipped with a variety of different insertases and translocases. Many of them are specialized, taking care of the export of only a few protein substrates, while others have more general roles. Here, we focus on the three general export/insertion pathways, the secretory (Sec) pathway, YidC and the twin-arginine translocation (TAT) pathway, focusing closely on the Escherichia coli (E. coli) paradigm. We only briefly mention dedicated export pathways found in different Gram-negative bacteria. The Sec system deals with the majority of exported proteins and functions both as a translocase for secretory proteins and an insertase for membrane proteins. The insertase YidC assists the Sec system or operates independently on membrane protein clients. Sec and YidC, in common with most export pathways, require their protein clients to be in soluble non-folded states to fit through the translocation channels and grooves. The TAT pathway is an exception, as it translocates folded proteins, some loaded with prosthetic groups.

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Abbreviations

APH:

Amphipathic helix

BAM:

Β-barrel assembly machinery

CU:

Chaperone-Usher

E. coli :

Escherichia coli

IRA:

Intramolecular regulator of ATPase

MD:

Mature domain

MTS:

Mature domain targeting signal

NBD:

Nucleotide binding domain

OMVs:

Outer membrane vesicles

PBD:

Preprotein binding domain

PMF:

Proton motive force

prl :

Protein localization

REMPs:

Redox enzyme maturation proteins

RNC:

Ribosome-nascent chain complex

SD:

Scaffold domain

Sec pathway:

Secretory pathway

SP:

Signal peptide

SRP:

Signal recognition particle

TAM:

Translocation and assembly module

TAT:

Twin-arginine translocation

TF:

Trigger factor

TMH:

Transmembrane helix

TXSS:

Type X secretion system

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Acknowledgements

Our research is funded through the: Research Foundation Flanders (FWO) [grant #G.0B49.15 (to SK); grant #G0C6814N RiMembR (to AE); FWO/F.R.S.-FNRS “Excellence of Science-EOS” programme grant #30550343 (to AE)], EU (FP7 KBBE.2013.3.6-02: Synthetic Biology towards applications; #613877 StrepSynth; to AE), RUN (#RUN/16/001 KU Leuven; to AE) and C1 (ZKD4582—C16/18/008 KU Leuven; to SK and AE). JDG is an FWO doctoral fellow.

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  1. Laboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, KU Leuven – University of Leuven, Herestraat 49, 3000, Leuven, Belgium

    Jozefien De Geyter, Dries Smets, Spyridoula Karamanou & Anastassios Economou

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  1. Jozefien De Geyter
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Correspondence to Anastassios Economou .

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  1. Inst. of Microbiology, University of Hohenheim, Stuttgart, Germany

    Andreas Kuhn

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De Geyter, J., Smets, D., Karamanou, S., Economou, A. (2019). Inner Membrane Translocases and Insertases. In: Kuhn, A. (eds) Bacterial Cell Walls and Membranes . Subcellular Biochemistry, vol 92. Springer, Cham. https://doi.org/10.1007/978-3-030-18768-2_11

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