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Inner Membrane Translocases and Insertases

Chapter
First Online:
Part of the Subcellular Biochemistry book series (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.

Keywords

Protein secretion Membrane insertion Inner membrane Sec YidC TAT Signal peptide Translocation Protein folding Export pathways Co-translational Post-translational Chaperones 

List of 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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Notes

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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Authors and Affiliations

  1. 1.Laboratory of Molecular Bacteriology, Department of Microbiology and ImmunologyRega Institute for Medical Research, KU Leuven – University of LeuvenLeuvenBelgium

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