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Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents
The important biological macromolecules, such as lipopeptide and glycolipid biosurfactant producing marine actinobacteria were analyzed and their potential linkage between type II polyketide synthase (PKS) genes was explored. A unique feature of type II PKS genes is their high amino acid (AA) sequen...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751271/ https://www.ncbi.nlm.nih.gov/pubmed/26903957 http://dx.doi.org/10.3389/fmicb.2016.00063 |
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author | Selvin, Joseph Sathiyanarayanan, Ganesan Lipton, Anuj N. Al-Dhabi, Naif Abdullah Valan Arasu, Mariadhas Kiran, George S. |
author_facet | Selvin, Joseph Sathiyanarayanan, Ganesan Lipton, Anuj N. Al-Dhabi, Naif Abdullah Valan Arasu, Mariadhas Kiran, George S. |
author_sort | Selvin, Joseph |
collection | PubMed |
description | The important biological macromolecules, such as lipopeptide and glycolipid biosurfactant producing marine actinobacteria were analyzed and their potential linkage between type II polyketide synthase (PKS) genes was explored. A unique feature of type II PKS genes is their high amino acid (AA) sequence homology and conserved gene organization. These enzymes mediate the biosynthesis of polyketide natural products with enormous structural complexity and chemical nature by combinatorial use of various domains. Therefore, deciphering the order of AA sequence encoded by PKS domains tailored the chemical structure of polyketide analogs still remains a great challenge. The present work deals with an in vitro and in silico analysis of PKS type II genes from five actinobacterial species to correlate KS domain architecture and structural features. Our present analysis reveals the unique protein domain organization of iterative type II PKS and KS domain of marine actinobacteria. The findings of this study would have implications in metabolic pathway reconstruction and design of semi-synthetic genomes to achieve rational design of novel natural products. |
format | Online Article Text |
id | pubmed-4751271 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-47512712016-02-22 Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents Selvin, Joseph Sathiyanarayanan, Ganesan Lipton, Anuj N. Al-Dhabi, Naif Abdullah Valan Arasu, Mariadhas Kiran, George S. Front Microbiol Microbiology The important biological macromolecules, such as lipopeptide and glycolipid biosurfactant producing marine actinobacteria were analyzed and their potential linkage between type II polyketide synthase (PKS) genes was explored. A unique feature of type II PKS genes is their high amino acid (AA) sequence homology and conserved gene organization. These enzymes mediate the biosynthesis of polyketide natural products with enormous structural complexity and chemical nature by combinatorial use of various domains. Therefore, deciphering the order of AA sequence encoded by PKS domains tailored the chemical structure of polyketide analogs still remains a great challenge. The present work deals with an in vitro and in silico analysis of PKS type II genes from five actinobacterial species to correlate KS domain architecture and structural features. Our present analysis reveals the unique protein domain organization of iterative type II PKS and KS domain of marine actinobacteria. The findings of this study would have implications in metabolic pathway reconstruction and design of semi-synthetic genomes to achieve rational design of novel natural products. Frontiers Media S.A. 2016-02-12 /pmc/articles/PMC4751271/ /pubmed/26903957 http://dx.doi.org/10.3389/fmicb.2016.00063 Text en Copyright © 2016 Selvin, Sathiyanarayanan, Lipton, Al-Dhabi, Valan Arasu and Kiran. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Selvin, Joseph Sathiyanarayanan, Ganesan Lipton, Anuj N. Al-Dhabi, Naif Abdullah Valan Arasu, Mariadhas Kiran, George S. Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents |
title | Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents |
title_full | Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents |
title_fullStr | Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents |
title_full_unstemmed | Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents |
title_short | Ketide Synthase (KS) Domain Prediction and Analysis of Iterative Type II PKS Gene in Marine Sponge-Associated Actinobacteria Producing Biosurfactants and Antimicrobial Agents |
title_sort | ketide synthase (ks) domain prediction and analysis of iterative type ii pks gene in marine sponge-associated actinobacteria producing biosurfactants and antimicrobial agents |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751271/ https://www.ncbi.nlm.nih.gov/pubmed/26903957 http://dx.doi.org/10.3389/fmicb.2016.00063 |
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