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Peer-reviewedCC BY-NC-ND 4.0Proceedings of the National Academy of Sciences of the United States of America

Signal peptides for engineered protein secretion by free and hydrogel-encapsulated cyanobacteria

  • Nathan T. Soulier1,2
  • Debika Datta2,3
  • Rakefet Schwarz4
  • Jonathan K. Pokorski2,3,5
  • James W. Golden1,2
  • Susan S. Golden1,2
5 affiliations
  1. 1Department of Molecular Biology, University of California San Diego, La Jolla, CA 92093
  2. 2Materials Science and Engineering Program, University of California San Diego, La Jolla, CA 92093
  3. 3Aiiso Yufeng Li Family Department of Chemical and Nano Engineering, University of California San Diego, La Jolla, CA 92093
  4. 4The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 5290002, Israel
  5. 5Institute for Materials Discovery and Design, University of California San Diego, La Jolla, CA 92093
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Abstract

Cyanobacteria provide a promising platform for light-driven heterologous protein production. In heterologous production systems, cells are typically lysed for product purification or to facilitate interaction with external substrates, unless the product is secreted. Fusion to molecular “shipping labels” known as signal peptides can target chimeric proteins to native membrane translocation pathways and result in secretion. In this work, we identified signal peptides from the model cyanobacterium Synechococcus elongatus PCC 7942 (S. elongatus) and genetically fused to two heterologous enzymes: the reporter nanoluciferase (NLuc) and an oxidative laccase (CotA). Increased extracellular activity was observed for one or more signal-protein variants for both enzymes. Furthermore, cells of S. elongatus producing a signal-laccase chimera were encapsulated within an alginate hydrogel, and the resulting engineered living material released sufficient enzyme to decolorize a dye pollutant in its surroundings. These findings streamline recombinant protein production in cyanobacteria and facilitate environmental interactions with cell products, expanding the potential applications of both free-living and material-encapsulated cyanobacteria.

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Cite

BibTeXRIS
BibTeX
@article{soulier2026signal,
  title = {{Signal peptides for engineered protein secretion by free and hydrogel-encapsulated cyanobacteria}},
  author = {Nathan T. Soulier and Debika Datta and Rakefet Schwarz and Jonathan K. Pokorski and James W. Golden and Susan S. Golden},
  journal = {Proceedings of the National Academy of Sciences of the United States of America},
  year = {2026},
  month = oct,
  doi = {10.1073/pnas.2624792123},
  url = {https://doi.org/10.1073/pnas.2624792123},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Signal peptides for engineered protein secretion by free and hydrogel-encapsulated cyanobacteria
AU  - Nathan T. Soulier
AU  - Debika Datta
AU  - Rakefet Schwarz
AU  - Jonathan K. Pokorski
AU  - James W. Golden
AU  - Susan S. Golden
PY  - 2026
DA  - 2026/10/21
JO  - Proceedings of the National Academy of Sciences of the United States of America
DO  - 10.1073/pnas.2624792123
UR  - https://doi.org/10.1073/pnas.2624792123
AB  - Cyanobacteria provide a promising platform for light-driven heterologous protein production. In heterologous production systems, cells are typically lysed for product purification or to facilitate interaction with external substrates, unless the product is secreted. Fusion to molecular “shipping labels” known as signal peptides can target chimeric proteins to native membrane translocation pathways and result in secretion. In this work, we identified signal peptides from the model cyanobacterium Synechococcus elongatus PCC 7942 (S. elongatus) and genetically fused to two heterologous enzymes: the reporter nanoluciferase (NLuc) and an oxidative laccase (CotA). Increased extracellular activity was observed for one or more signal-protein variants for both enzymes. Furthermore, cells of S. elongatus producing a signal-laccase chimera were encapsulated within an alginate hydrogel, and the resulting engineered living material released sufficient enzyme to decolorize a dye pollutant in its surroundings. These findings streamline recombinant protein production in cyanobacteria and facilitate environmental interactions with cell products, expanding the potential applications of both free-living and material-encapsulated cyanobacteria.
SN  - 0027-8424
SN  - 1091-6490
ER  -