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  • Review Article
  • Published:

Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases

Nature Reviews Microbiology volume 6, pages 234–244 (2008)Cite this article

An Erratum to this article was published on 11 December 2017

This article has been updated

Key Points

  • General introduction to bacterial membrane protein insertion and the Sec translocases.

  • Membrane protein topology and targeting to the membrane.

  • 'YidC-only' pathway for bacterial membrane protein insertion.

  • YidC family members and their structure function.

  • Bacterial Sec pathway for membrane protein insertion and comparison with the eukaryotic Sec system in the endoplasmic reticulum.

  • SecYEG structure.

  • Folding, assembly and quality control of bacterial membrane proteins.

  • Conclusion: resolved problems and open questions.

Abstract

This Review describes the pathways that are used to insert newly synthesized proteins into the cytoplasmic membranes of bacteria, and provides insight into the function of two of the evolutionarily conserved translocases that catalyse this process. These highly sophisticated translocases are responsible for decoding the topogenic sequences within membrane proteins that direct membrane protein insertion and orientation. The role of the Sec and YidC translocases in the folding of bacterial membrane proteins is also highlighted.

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Figure 1: The machinery that is involved in membrane protein insertion.
Figure 2: Membrane insertion of the lipoprotein CyoA.
Figure 3: The interaction of YidC with TM segments.
Figure 4: The SecYEβ structure and the lateral gate.

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Change history

  • 11 December 2017

    This article was published with an incorrect DOI. The correct DOI is 10.1038/nrmicro3595. This has now been corrected in the online version. We apologize to the authors and to readers for any confusion caused.

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Acknowledgements

Work in the laboratory of R.E.D. was supported by National Institutes of Health Grant GM63862-05. The authors thank A. Kuhn for critical reading of the manuscript.

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Authors and Affiliations

  1. Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, 43210, Ohio, USA

    Kun Xie & Ross E. Dalbey

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  1. Kun Xie
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Correspondence to Ross E. Dalbey.

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DATABASES

Entrez Genome Project

Bacillus subtilis

Escherichia coli

Methanococcus jannaschii

Neisseria meningitidis

Neurospora crassa

Rhodobacter capsulatus

Streptococcus mutans

Entrez Protein

Omp85

SecA

SecB

SecE

SecF

SecG

SecY

YaeT

YajC

YfgL

YidC

FURTHER INFORMATION

Ross E. Dalbey's homepage

Glossary

Type I membrane protein

A protein which contains a single membrane-spanning domain that has its carboxyl terminus orientated towards the cytoplasm and its amino terminus orientated towards the lumen of membrane compartments or in an extracellular direction.

Type II membrane protein

A single-spanning membrane protein that has the opposite topology to a type I membrane protein.

Signal-recognition particle

A complex that is responsible for targeting nascent polypeptides to the cell membranes, and identifies an amino-terminal signal sequence that is carried by proteins that are destined for secretion or membrane localization.

Two-partner secretion system

A secretion system that is composed of two distinct proteins; one is secreted and the other is its transporter.

Signal anchor

A topogenic sequence that signals the initiation of translocation of the carboxy-terminal region of a membrane protein, and remains as a membrane anchor with an NinCout orientation. Also known as a type II signal anchor.

Reverse signal anchor

A topogenic sequence that signals the initiation of translocation of the amino-terminal region of a membrane protein, and remains as a membrane-spanning region that has an NoutCin orientation. Also known as a type I signal anchor.

Signal peptidase II

A signal peptidase that proteolytically removes lipoprotein signal sequences.

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Xie, K., Dalbey, R. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat Rev Microbiol 6, 234–244 (2008). https://doi.org/10.1038/nrmicro3595

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