Cited by 211Bacterial Genetics and BiotechnologyLipid Membrane Structure and BehaviorHeat shock proteins research

Escherichia coli YidC is a membrane insertase for Sec-independent proteins.

Open access
Serek, Justyna, Bauer‐Manz, Gabriele, Struhalla, Gabriele, van den Berg, Lambertus, Kiefer, Dorothee, Dalbey, Ross, Kuhn, Andreas·2004·The EMBO Journal

Abstract

YidC is a recently discovered bacterial membrane protein that is related to the mitochondrial Oxa1p and the Alb3 protein of chloroplasts. These proteins are required in the membrane integration process of newly synthesized proteins that do not require the classical Sec machinery. Here we demonstrate that YidC is sufficient for the membrane integration of a Sec-independent protein. Microgram amounts of the purified single-spanning Pf3 coat protein were efficiently inserted into proteoliposomes containing the purified YidC. A mutant Pf3 coat protein with an extended hydrophobic region was inserted independently of YidC into the membrane both in vivo and in vitro, but its insertion was accelerated by YidC. These results show that YidC can function separately from the Sec translocase to integrate membrane proteins into the lipid bilayer.

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Crossref · 10.1038/sj.emboj.7600063

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  • Although YidC can act as a SecYEG-independent insertase for some membrane proteins, it also associates with the SecYEG complex.

    “Although YidC can act as SecYEG-independent insertase for some membrane proteins (Samuelson et al., 2000; Luirink et al., 2001; Serek et al., 2004; Welte et al., 2012), it also associates with the SecYEG complex (Scotti et al., 2000; Nouwen and Driessen, 2002; Li et al., 2013; Sachelaru et al., 2015, 2017).”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Serek et al., 2004

  • Membrane proteins that cannot engage YidC as a second integration site are strictly dependent on SecYEG.

    “Intriguingly, these membrane proteins cannot engage YidC as second integration site for membrane proteins (Samuelson et al., 2000; Serek et al., 2004) and are therefore strictly dependent on SecYEG.”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Serek et al., 2004

  • YidC is an evolutionarily conserved protein that is required for the growth of E. coli.

    “YidC represents an evolutionarily conserved protein that is required for the growth of E. coli [88,89].”

    From Effect of essential oils on pathogenic bacteria (2013) · cites this paper as [88]

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Authors
Serek, J., Bauer‐Manz, G., Struhalla, G., van den Berg, L., Kiefer, D., Dalbey, R., & Kuhn, A.
Affiliations
  • University of Hohenheim (DE)
  • The Ohio State University (US)
Venue
The EMBO Journal
Published
2004-01-22
Volume
23
Issue
2
Pages
294-301
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W2033534477
Cited by
211
References
39
Citations by year
2026: 3 · 2025: 3 · 2024: 4 · 2023: 4 · 2022: 11 · 2021: 10 · 2020: 4 · 2019: 14 · 2018: 6 · 2017: 7 · 2016: 2 · 2015: 5 · 2014: 11 · 2013: 11 · 2012: 13
FWCI
8.57
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Deutsche Forschungsgemeinschaft
  • National Institutes of Health (GM63862)
  • National Institute of General Medical Sciences (GM 63862, R01GM063862)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
YidC, proteoliposomes, hydrophobic region, Escherichia coli
MeSH terms
SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Proteins, Liposomes, Proteolipids, Membrane Transport Proteins, Escherichia coli Proteins, Capsid Proteins

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