Structural diversity in twin-arginine signal peptide-binding proteins
Open accessAbstract
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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The mononuclear molybdenum enzymes
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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
- Publisher
- National Academy of Sciences
- Published
- 2007-10-02
- Volume
- 104
- Issue
- 40
- Pages
- 15641-15646
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2000414
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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