Cited by 65Bacterial Genetics and BiotechnologyRNA and protein synthesis mechanismsCellular transport and secretion

Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.

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Ishii, Eiji, Chiba, Shinobu, Hashimoto, Narimasa, Kojima, Seiji, Homma, Michio, Ito, Koreaki, Akiyama, Yoshinori, Mori, Hiroyuki·2015·Proceedings of the National Academy of Sciences

Abstract

Significance: Bacteria living in seawater must cope with low-sodium environments that they may encounter. Here we show an unexpected finding that remodeling of the Sec protein export machinery plays a pivotal role in this adaptation. Vibrio alginolyticus possesses alternative SecDF1 and SecDF2 homologs that use the transmembrane gradient of Na + and that of H + , respectively, to enhance protein export by cooperating with the SecYEG translocon. The synthesis of SecDF2 is induced in low-Na + environments, and this induction is essential for the bacterium to survive low salinity. Remarkably, the Vibrio species use a nascent polypeptide, VemP, to monitor the functional state of the Sec pathway and to up-regulate translation of SecDF2 when activity of the SecDF1-containing Sec machinery declines.

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Crossref · 10.1073/pnas.1513001112

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  • In Vibrio alginolyticus, the substrate VemP controls the switch between a sodium-coupled SecDF2 complex and a proton-coupled SecDF1 complex in low Na+ environments.

    “The use of monitoring substrates for adjusting the protein transport capacity has also been shown in Vibrio alginolyticus, where the substrate VemP controls the switch between a sodium-coupled SecDF2 complex and a proton-coupled SecDF1 complex in low Na+ environments (Ishii et al., 2015; Miyazaki et al., 2020).”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Ishii et al., 2015

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Authors
Ishii, E., Chiba, S., Hashimoto, N., Kojima, S., Homma, M., Ito, K., Akiyama, Y., & Mori, H.
Affiliations
  • Kyoto University (JP)
  • Kyoto Sangyo University (JP)
  • Nagoya University (JP)
Corresponding author
Mori, Hiroyuki
Venue
Proceedings of the National Academy of Sciences
Published
2015-09-21
Volume
112
Issue
40
Pages
E5513-22
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2150104949
Cited by
65
References
73
Citations by year
2026: 3 · 2025: 4 · 2024: 11 · 2023: 7 · 2022: 6 · 2021: 8 · 2020: 6 · 2019: 2 · 2018: 8 · 2017: 5 · 2016: 5
FWCI
4.11
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Ministry of Education, Culture, Sports, Science, and Technology (24117003, 15H01532, 26116008)
  • Japan Society for the Promotion of Science (22370070, 25291006)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
SecDF, SecYEG translocon, protein export, Vibrio alginolyticus, salinity adaptation, proton motive force, vestibular evoked myogenic potentials, gene expression regulation, marine bacteria, paralogs
MeSH terms
Amino Acid Sequence, Bacterial Proteins, Base Sequence, Molecular Sequence Data, Mutation, Nucleic Acid Conformation, Ribosomes, RNA, Messenger, Seawater, Sodium, Protein Biosynthesis, Vibrio, Immunoblotting, Gene Expression Regulation, Bacterial, Sequence Homology, Amino Acid, Proton-Motive Force, Protein Transport, Salinity, Salt Tolerance

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