Genomic insights into cyanobacterial protein translocation systems
Author:
Russo David A.1ORCID, Zedler Julie A. Z.2ORCID
Affiliation:
1. Bioorganic Analytics , Institute for Inorganic and Analytical Chemistry, Friedrich Schiller University Jena , D-07743 Jena , Germany 2. Matthias Schleiden Institute for Genetics, Bioinformatics and Molecular Botany, Friedrich Schiller University Jena , Dornburgerstr. 159 , D-07743 Jena , Germany
Abstract
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.
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Reference123 articles.
1. Abby, S.S., Cury, J., Guglielmini, J., Néron, B., Touchon, M., and Rocha, E.P.C. (2016). Identification of protein secretion systems in bacterial genomes. Sci. Rep. 6: 23080, https://doi.org/10.1038/srep23080. 2. Abby, S.S., Néron, B., Ménager, H., Touchon, M., and Rocha, E.P.C. (2014). MacSyFinder: a program to mine genomes for molecular systems with an application to CRISPR-Cas systems. PloS One 9: e110726, https://doi.org/10.1371/journal.pone.0110726. 3. Agarwal, R., Zakharov, S., Hasan, S.S., Ryan, C.M., Whitelegge, J.P., and Cramer, W.A. (2014). Structure-function of cyanobacterial outer-membrane protein, Slr1270: homolog of Escherichia coli drug export/colicin import protein. TolC. FEBS Lett. 588: 3793–3801, https://doi.org/10.1016/j.febslet.2014.08.028. 4. Akimaru, J., Matsuyama, S., Tokuda, H., and Mizushima, S. (1991). Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 88: 6545–6549, https://doi.org/10.1073/pnas.88.15.6545. 5. Akoh, C.C., Lee, G.-C., Liaw, Y.-C., Huang, T.-H., and Shaw, J.-F. (2004). GDSL family of serine esterases/lipases. Prog. Lipid Res. 43: 534–552, https://doi.org/10.1016/j.plipres.2004.09.002.
Cited by
12 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|