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Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins
Polyhydroxyalkanoates (PHAs) are natural polyesters of increasing biotechnological importance that are synthesized by many prokaryotic organisms as carbon and energy storage compounds in limiting growth conditions. PHAs accumulate intracellularly in form of inclusion bodies that are covered with a p...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5658603/ https://www.ncbi.nlm.nih.gov/pubmed/28425176 http://dx.doi.org/10.1111/1751-7915.12718 |
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author | Maestro, Beatriz Sanz, Jesús M. |
author_facet | Maestro, Beatriz Sanz, Jesús M. |
author_sort | Maestro, Beatriz |
collection | PubMed |
description | Polyhydroxyalkanoates (PHAs) are natural polyesters of increasing biotechnological importance that are synthesized by many prokaryotic organisms as carbon and energy storage compounds in limiting growth conditions. PHAs accumulate intracellularly in form of inclusion bodies that are covered with a proteinaceous surface layer (granule‐associated proteins or GAPs) conforming a network‐like surface of structural, metabolic and regulatory polypeptides, and configuring the PHA granules as complex and well‐organized subcellular structures that have been designated as ‘carbonosomes’. GAPs include several enzymes related to PHA metabolism (synthases, depolymerases and hydroxylases) together with the so‐called phasins, an heterogeneous group of small‐size proteins that cover most of the PHA granule and that are devoid of catalytic functions but nevertheless play an essential role in granule structure and PHA metabolism. Structurally, phasins are amphiphilic proteins that shield the hydrophobic polymer from the cytoplasm. Here, we summarize the characteristics of the different phasins identified so far from PHA producer organisms and highlight the diverse opportunities that they offer in the Biotechnology field. |
format | Online Article Text |
id | pubmed-5658603 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-56586032017-11-01 Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins Maestro, Beatriz Sanz, Jesús M. Microb Biotechnol Minireviews Polyhydroxyalkanoates (PHAs) are natural polyesters of increasing biotechnological importance that are synthesized by many prokaryotic organisms as carbon and energy storage compounds in limiting growth conditions. PHAs accumulate intracellularly in form of inclusion bodies that are covered with a proteinaceous surface layer (granule‐associated proteins or GAPs) conforming a network‐like surface of structural, metabolic and regulatory polypeptides, and configuring the PHA granules as complex and well‐organized subcellular structures that have been designated as ‘carbonosomes’. GAPs include several enzymes related to PHA metabolism (synthases, depolymerases and hydroxylases) together with the so‐called phasins, an heterogeneous group of small‐size proteins that cover most of the PHA granule and that are devoid of catalytic functions but nevertheless play an essential role in granule structure and PHA metabolism. Structurally, phasins are amphiphilic proteins that shield the hydrophobic polymer from the cytoplasm. Here, we summarize the characteristics of the different phasins identified so far from PHA producer organisms and highlight the diverse opportunities that they offer in the Biotechnology field. John Wiley and Sons Inc. 2017-04-20 /pmc/articles/PMC5658603/ /pubmed/28425176 http://dx.doi.org/10.1111/1751-7915.12718 Text en © 2017 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Minireviews Maestro, Beatriz Sanz, Jesús M. Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
title | Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
title_full | Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
title_fullStr | Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
title_full_unstemmed | Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
title_short | Polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
title_sort | polyhydroxyalkanoate‐associated phasins as phylogenetically heterogeneous, multipurpose proteins |
topic | Minireviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5658603/ https://www.ncbi.nlm.nih.gov/pubmed/28425176 http://dx.doi.org/10.1111/1751-7915.12718 |
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