Identification of the Streptomyces aculeolatus proteins involved in the biosynthesis of bioactive compound by a comparative 2D electrophoresis approach

Event Abstract Back to Event Identification of the Streptomyces aculeolatus proteins involved in the biosynthesis of bioactive compound by a comparative 2D electrophoresis approach Ana F. Fernandes1, 2, 3*, Lígia Costa1, 2, 3*, Ilda Santos-Sanches1, Susana P. Gaudêncio1, 3 and M. Gabriela Almeida2, 4 1 UCIBIO-REQUIMTE, Department of Life Sciences, Faculty of Science and Technology, Universidade NOVA de Lisboa, Portugal 2 UCIBIO-REQUIMTE, Department of Chemistry, Faculty of Science and Technology, Universidade NOVA de Lisboa, Portugal 3 LAQV-REQUIMTE, Department of Chemistry, Faculty of Science and Technology, Universidade NOVA de Lisboa, Portugal 4 Centro de Investigação Interdisciplinar Egas Moniz - Instituto Superior de Ciências de Saúde Egas Moniz, Portugal Actinomycetes Streptomyces aculeolatus belong to MAR4 streptomycete lineage and are known to produce hybrid isoprenoids including a naphthoquionone moiety, such as napyradiomycin and marinone families, a phthalazinone core as in azamerone class, and a phenazine moiety as in lavanducyanin and marinophenazine families.[1] These compounds have great bioactive potential as antibacterial, antifungal, and anticancer agents making them attractive leads to the pharmaceutical industry.[1],[2],[3] A total of 421 actinomycetes were isolated from marine sediments collected from the Madeira Archipelago, six of these belong to the S. aculeolatus specie, as determined by a phylogenetic analysis based on the sequencing of the gene 16S rRNA. These strains (coded PTM-29, PTM-81, PTM-129, PTM-346, PTM-398 and PTM-420) revealed the production of secondary metabolites with distinct bioactivities. In this context, we aim at characterizing the proteins involved in the synthesis of the main bioactive compounds at the strains PTM-29, PTM-129, PTM-346 and PTM-398. To achieve this goal, we are following a differential proteomic analysis based in two-dimensional electrophoresis (2DE) followed by mass spectrometry techniques (MS). The total and extracellular proteome of S. aculeolatus strains were analysed in the pH range 4-7, in 12,5% acrylamide gels stained with Colloidal Commassie Blue. Preliminary results showed similar protein profiles for the total proteomes, with most of the spots in the pH range 5-7 and a high molecular weight (above 50 kDa). Curiously, the extracellular proteomes have shown to be very different among strains, also presenting high molecular weight proteins. As future work, we intend to analyse in detail the 2D gels from the S. aculeolatus strains in study and identify the differentially expressed proteins by mass spectrometry (MS) techniques. Acknowledgements This research is the result of financial support from Fundação para a Ciência e a Tecnologia (FCT) and FEDER through grant PTDC/QUI-QUI/119116/2010, IF/00700/2014, PEst-C/EQB/LA0006/2013, UID/QUI/50006/2013 and UID/Multi/04378/2013, and the European Union 7th Framework Programme (FP7/2007-2013) under grant agreement PCOFUND-GA-2009-246542 and 269138-NanoGuard, and grant Instruct Access1153. References [1] K. A. Gallagher and P. R. Jensen, “Genomic insights into the evolution of hybrid isoprenoid biosynthetic gene clusters in the MAR4 marine streptomycete clade.,” BMC Genomics, 16(960), 1-13, 2015. [2] Y. Bin Cheng, P. R. Jensen, and W. Fenical, “Cytotoxic and antimicrobial napyradiomycins from two marine-derived streptomyces strains,” European J. Org. Chem., 3751–3757, 2013. [3] US4904590-A ; EP376609-A ; CA2006342-A ; JP2258774-A ; EP376609-B1 ; DE68918071-E ; ES2059791-T3. Keywords: Streptomyces aculeolatus, MAR4, Actinomycetes, bioactive compounds, Proteins Conference: IMMR | International Meeting on Marine Research 2016, Peniche, Portugal, 14 Jul - 15 Jul, 2016. Presentation Type: Poster presentation Topic: Blue Biotechnology Citation: Fernandes AF, Costa L, Santos-Sanches I, Gaudêncio SP and Almeida M (2016). Identification of the Streptomyces aculeolatus proteins involved in the biosynthesis of bioactive compound by a comparative 2D electrophoresis approach. Front. Mar. Sci. Conference Abstract: IMMR | International Meeting on Marine Research 2016. doi: 10.3389/conf.FMARS.2016.04.00057 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 18 Apr 2016; Published Online: 13 Jul 2016. * Correspondence: Miss. Ana F Fernandes, UCIBIO-REQUIMTE, Department of Life Sciences, Faculty of Science and Technology, Universidade NOVA de Lisboa, Caparica, 2829-516, Portugal, af.fernandes@campus.fct.unl.pt Miss. Lígia Costa, UCIBIO-REQUIMTE, Department of Life Sciences, Faculty of Science and Technology, Universidade NOVA de Lisboa, Caparica, 2829-516, Portugal, lfr.costa@campus.fct.unl.pt Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Ana F Fernandes Lígia Costa Ilda Santos-Sanches Susana P Gaudêncio M. Gabriela Almeida Google Ana F Fernandes Lígia Costa Ilda Santos-Sanches Susana P Gaudêncio M. Gabriela Almeida Google Scholar Ana F Fernandes Lígia Costa Ilda Santos-Sanches Susana P Gaudêncio M. Gabriela Almeida PubMed Ana F Fernandes Lígia Costa Ilda Santos-Sanches Susana P Gaudêncio M. Gabriela Almeida Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.