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Genomic insights into cyanobacterial protein translocation systems

  • David A. Russo ORCID logo and Julie A. Z. Zedler ORCID logo EMAIL logo
Published/Copyright: October 12, 2020
Biological Chemistry
From the journal Biological Chemistry Volume 402 Issue 1

Abstract

Cyanobacteria are ubiquitous oxygenic photosynthetic bacteria with a versatile metabolism that is highly dependent on effective protein targeting. Protein sorting in diderm bacteria is not trivial and, in cyanobacteria, even less so due to the presence of a complex membrane system: the outer membrane, the plasma membrane and the thylakoid membrane. In cyanobacteria, protein import into the thylakoids is essential for photosynthesis, export to the periplasm fulfills a multifunctional role in maintaining cell homeostasis, and secretion mediates motility, DNA uptake and environmental interactions. Intriguingly, only one set of genes for the general secretory and the twin-arginine translocation pathways seem to be present. However, these systems have to operate in both plasma and thylakoid membranes. This raises the question of how substrates are recognized and targeted to their correct, final destination. Additional complexities arise when a protein has to be secreted across the outer membrane, where very little is known regarding the mechanisms involved. Given their ecological importance and biotechnological interest, a better understanding of protein targeting in cyanobacteria is of great value. This review will provide insights into the known knowns of protein targeting, propose hypotheses based on available genomic sequences and discuss future directions.

Keywords: bacterial protein secretion; cyanobacteria; protein sorting; protein targeting; sec pathway; twin-arginine translocation pathway
Corresponding author: Julie A. Z. Zedler, Matthias Schleiden Institute for Genetics, Bioinformatics and Molecular Botany, Friedrich Schiller University Jena, Dornburgerstr. 159, D-07743 Jena, Germany, E-mail:

Acknowledgments

We would like to thank Michael A. Russo for assistance with database generation, Dr. Sophie S. Abby for assistance with MacSyFinder and Prof. Conrad W. Mullineaux for interesting discussions on protein targeting.

  1. Author contribution: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: None declared.

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Supplementary Material

The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2020-0247).

Received: 2020-07-09
Accepted: 2020-09-25
Published Online: 2020-10-12
Published in Print: 2020-11-18

© 2020 Walter de Gruyter GmbH, Berlin/Boston

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  2. Publisher’s Note
  3. Editorial
  4. Douglas D. Thomas named next Editor-in-Chief of Biological Chemistry
  5. Guest Editorial
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  7. Highlight: GBM Young Investigators (Part 3)
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https://doi.org/10.1515/hsz-2020-0247
Keywords for this article
bacterial protein secretion; cyanobacteria; protein sorting; protein targeting; sec pathway; twin-arginine translocation pathway

Articles in the same Issue

  1. Frontmatter
  2. Publisher’s Note
  3. Editorial
  4. Douglas D. Thomas named next Editor-in-Chief of Biological Chemistry
  5. Guest Editorial
  6. Highlight: young research groups in Germany – 3rd edition
  7. Highlight: GBM Young Investigators (Part 3)
  8. LOTUS-domain proteins - developmental effectors from a molecular perspective
  9. The role of very long chain fatty acids in yeast physiology and human diseases
  10. Genomic insights into cyanobacterial protein translocation systems
  11. An RNA-centric view on gut Bacteroidetes
  12. Kill one or kill the many: interplay between mitophagy and apoptosis
  13. RNA secondary structure dependence in METTL3–METTL14 mRNA methylation is modulated by the N-terminal domain of METTL3
  14. Influence of monovalent metal ions on metal binding and catalytic activity of the 10–23 DNAzyme
  15. Integrated Ca2+ flux and AFM force analysis in human iPSC-derived cardiomyocytes
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