ArticleMolecular biotechnology2015
Exploring the Feasibility of the Sec Route to Secrete Proteins Using the Tat Route in Streptomyces lividans.
Article in Molecular biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Enhanced production of neoagarobiose from agar with Corynebacterium glutamicum producing exo-type and endo-type β-agarases.Microbial biotechnology · 2021Article
- Review
- Streptomycetes: Attractive Hosts for Recombinant Protein Production.Frontiers in microbiology · 2020Review
- Functional identification of aOpen biology · 2019Article
- Dynamic metabolic modelling of overproduced protein secretion in Streptomyces lividans using adaptive DFBA.BMC microbiology · 2019Article
- Modelling the metabolism of protein secretion through the Tat route in Streptomyces lividans.BMC microbiology · 2018Article
- The Cellular Mechanisms that Ensure an Efficient Secretion in Streptomyces.Antibiotics (Basel, Switzerland) · 2018Review
- Monitoring Protein Secretion inFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptomyces lividans uses mainly two pathways to target secretory proteins to the cytoplasmic membrane. The major pathway (Sec pathway) transports pre-proteins using the signal recognition particle, and the minor Tat pathway is responsible for the secretion using a folded conformation of a relatively low number of proteins. The signal peptides of the Sec-dependent alpha-amylase and the Tat-dependent agarase were interchanged and fused in-frame to the corresponding mature part of the other enzyme. Alpha-amylase was unable to use the Tat route when fused to the agarase signal peptide, while agarase used the Sec route when it was targeted by the alpha-amylase signal peptide. In addition to the signal peptide some yet unidentified parts of the secreted proteins may play a role in selecting the secretory route. Structure predictions for the Tat- and Sec-dependent proteins suggest that less structured proteins are more likely to be candidates for the Tat route.
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Registered trials
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