Cited by 74Bacterial Genetics and BiotechnologyEnzyme Structure and FunctionProtein Structure and Dynamics

Structural diversity in twin-arginine signal peptide-binding proteins

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Maillard, Julien, Spronk, Chris A. E. M., Buchanan, Grant, Lyall, Verity, Richardson, David J., Palmer, Tracy, Vuister, Geerten W., Sargent, Frank·2007·Proceedings of the National Academy of Sciences

Abstract

The twin-arginine transport (Tat) system is dedicated to the translocation of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat system by signal peptides containing a twin-arginine motif. In Escherichia coli , many Tat substrates bind redox-active cofactors in the cytoplasm before transport. Coordination of cofactor insertion with protein export involves a “Tat proofreading” process in which chaperones bind twin-arginine signal peptides, thus preventing premature export. The initial Tat signal-binding proteins described belonged to the TorD family, which are required for assembly of N - and S -oxide reductases. Here, we report that E. coli NapD is a Tat signal peptide-binding chaperone involved in biosynthesis of the Tat-dependent nitrate reductase NapA. NapD binds tightly and specifically to the NapA twin-arginine signal peptide and suppresses signal peptide translocation activity such that transport via the Tat pathway is retarded. High-resolution, heteronuclear, multidimensional NMR spectroscopy reveals the 3D solution structure of NapD. The chaperone adopts a ferredoxin-type fold, which is completely distinct from the TorD family. Thus, NapD represents a new family of twin-arginine signal-peptide-binding proteins.

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  • NapD interacts with the twin arginine translocase (TAT) leader sequence of NapA and possibly other maturation proteins such as NapF in NapA biosynthesis.

    “It interacts with the twin arginine translocase (TAT) leader sequence of NapA and possibly other maturation proteins, such as NapF, in the biosynthesis of NapA.267”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [267]

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Authors
Maillard, J., Spronk, C. A. E. M., Buchanan, G., Lyall, V., Richardson, D. J., Palmer, T., Vuister, G. W., & Sargent, F.
Affiliations
  • University of East Anglia (GB)
  • Center for Molecular and Biomolecular Informatics, Nijmegen Center for Molecular Life Sciences, and
  • John Innes Centre (GB)
  • Radboud University Nijmegen (NL)
Venue
Proceedings of the National Academy of Sciences
Published
2007-10-02
Volume
104
Issue
40
Pages
15641-15646
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1984125384
Cited by
74
References
47
Citations by year
2026: 1 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 3 · 2018: 1 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 5 · 2012: 5
FWCI
5.53
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)
  • Discovery Research Portal (University of Dundee) (publishedVersion)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
  • Leicester Research Archive (University of Leicester) (submittedVersion)
  • Radboud Repository (Radboud University) (submittedVersion)
  • UEA Digital Repository (University of East Anglia) (submittedVersion)
Funders
  • Nederlandse Organisatie voor Wetenschappelijk Onderzoek (700.55.443)
  • Biotechnology and Biological Sciences Research Council (BBS/B/07780/2, BBS/B/07780)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
molecular chaperones, folded protein translocation, Escherichia coli, protein structure
MeSH terms
Arginine, Binding Sites, Carrier Proteins, Escherichia coli, Oxidation-Reduction, Protein Binding, Substrate Specificity, Genetic Variation, Signal Transduction, Protein Sorting Signals, Membrane Transport Proteins, Escherichia coli Proteins, Nitrate Reductase

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