ArticlePloS one2013
Effect of signal peptide on stability and folding of Escherichia coli thioredoxin.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 90 citations in OpenAlex.
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- Biomimetic peptide conjugates as emerging strategies for controlled release from protein-based materials.Drug delivery · 2025Review
- An inverse relationship between fitness and secretion efficiency in a gram-positive bacterium.PNAS nexus · 2025Article
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- Controlling tumor progression and recurrence in mice through combined treatment with a PD-L1 inhibitor and a designerActa pharmaceutica Sinica. B · 2024Article
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- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- Signal peptide stabilizes folding and inhibits misfolding of serum amyloid A.Protein science : a publication of the Protein Society · 2022Article
- Comparative Analysis of NanoLuc Luciferase and Alkaline Phosphatase Luminescence Reporter Systems for Phage-Based Detection of Bacteria.Bioengineering (Basel, Switzerland) · 2022Article
- Extracellular secretion of a cutinase with polyester-degrading potential by E. coli using a novel signal peptide from Amycolatopsis mediterranei.World journal of microbiology & biotechnology · 2022Article
- Different strategies for expression and purification of the CT26-poly-neoepitopes vaccine in Escherichia coli.Molecular biology reports · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Introduction of a Hexalysine (6 K) Tag Can Protect from N-Terminal Cleavage and Increase Yield of Recombinant Proteins Expressed in the Periplasm of E. coli.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Coexpressing the Signal Peptide of Vip3A and the Trigger Factor ofFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal peptide plays a key role in targeting and membrane insertion of secretory and membrane proteins in both prokaryotes and eukaryotes. In E. coli, recombinant proteins can be targeted to the periplasmic space by fusing naturally occurring signal sequences to their N-terminus. The model protein thioredoxin was fused at its N-terminus with malE and pelB signal sequences. While WT and the pelB fusion are soluble when expressed, the malE fusion was targeted to inclusion bodies and was refolded in vitro to yield a monomeric product with identical secondary structure to WT thioredoxin. The purified recombinant proteins were studied with respect to their thermodynamic stability, aggregation propensity and activity, and compared with wild type thioredoxin, without a signal sequence. The presence of signal sequences leads to thermodynamic destabilization, reduces the activity and increases the aggregation propensity, with malE having much larger effects than pelB. These studies show that besides acting as address labels, signal sequences can modulate protein stability and aggregation in a sequence dependent manner.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.