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Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization

Alginate-degrading bacteria play an important role in alginate degradation by harboring highly efficient and unique alginolytic genes. Although the general mechanism for alginate degradation by these bacteria is fairly understood, much is still required to fully exploit them. Here, we report the iso...

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Autores principales: Mori, Tetsushi, Takahashi, Mami, Tanaka, Reiji, Miyake, Hideo, Shibata, Toshiyuki, Chow, Seinen, Kuroda, Kouichi, Ueda, Mitsuyoshi, Takeyama, Haruko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4866713/
https://www.ncbi.nlm.nih.gov/pubmed/27176711
http://dx.doi.org/10.1371/journal.pone.0155537
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author Mori, Tetsushi
Takahashi, Mami
Tanaka, Reiji
Miyake, Hideo
Shibata, Toshiyuki
Chow, Seinen
Kuroda, Kouichi
Ueda, Mitsuyoshi
Takeyama, Haruko
author_facet Mori, Tetsushi
Takahashi, Mami
Tanaka, Reiji
Miyake, Hideo
Shibata, Toshiyuki
Chow, Seinen
Kuroda, Kouichi
Ueda, Mitsuyoshi
Takeyama, Haruko
author_sort Mori, Tetsushi
collection PubMed
description Alginate-degrading bacteria play an important role in alginate degradation by harboring highly efficient and unique alginolytic genes. Although the general mechanism for alginate degradation by these bacteria is fairly understood, much is still required to fully exploit them. Here, we report the isolation of a novel strain, Falsirhodobacter sp. alg1, the first report for an alginate-degrading bacterium from the family Rhodobacteraceae. Genome sequencing reveals that strain alg1 harbors a primary alginate degradation pathway with only single homologs of an endo- and exo-type alginate lyase, AlyFRA and AlyFRB, which is uncommon among such bacteria. Subsequent functional analysis showed that both enzymes were extremely efficient to depolymerize alginate suggesting evolutionary interests in the acquirement of these enzymes. The exo-type alginate lyase, AlyFRB in particular could depolymerize alginate without producing intermediate products making it a highly efficient enzyme for the production of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEH). Based on our findings, we believe that the discovery of Falsirhodobacter sp. alg1 and its alginolytic genes hints at the potentiality of a more diverse and unique population of alginate-degrading bacteria.
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spelling pubmed-48667132016-05-18 Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization Mori, Tetsushi Takahashi, Mami Tanaka, Reiji Miyake, Hideo Shibata, Toshiyuki Chow, Seinen Kuroda, Kouichi Ueda, Mitsuyoshi Takeyama, Haruko PLoS One Research Article Alginate-degrading bacteria play an important role in alginate degradation by harboring highly efficient and unique alginolytic genes. Although the general mechanism for alginate degradation by these bacteria is fairly understood, much is still required to fully exploit them. Here, we report the isolation of a novel strain, Falsirhodobacter sp. alg1, the first report for an alginate-degrading bacterium from the family Rhodobacteraceae. Genome sequencing reveals that strain alg1 harbors a primary alginate degradation pathway with only single homologs of an endo- and exo-type alginate lyase, AlyFRA and AlyFRB, which is uncommon among such bacteria. Subsequent functional analysis showed that both enzymes were extremely efficient to depolymerize alginate suggesting evolutionary interests in the acquirement of these enzymes. The exo-type alginate lyase, AlyFRB in particular could depolymerize alginate without producing intermediate products making it a highly efficient enzyme for the production of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEH). Based on our findings, we believe that the discovery of Falsirhodobacter sp. alg1 and its alginolytic genes hints at the potentiality of a more diverse and unique population of alginate-degrading bacteria. Public Library of Science 2016-05-13 /pmc/articles/PMC4866713/ /pubmed/27176711 http://dx.doi.org/10.1371/journal.pone.0155537 Text en © 2016 Mori et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Mori, Tetsushi
Takahashi, Mami
Tanaka, Reiji
Miyake, Hideo
Shibata, Toshiyuki
Chow, Seinen
Kuroda, Kouichi
Ueda, Mitsuyoshi
Takeyama, Haruko
Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization
title Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization
title_full Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization
title_fullStr Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization
title_full_unstemmed Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization
title_short Falsirhodobacter sp. alg1 Harbors Single Homologs of Endo and Exo-Type Alginate Lyases Efficient for Alginate Depolymerization
title_sort falsirhodobacter sp. alg1 harbors single homologs of endo and exo-type alginate lyases efficient for alginate depolymerization
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4866713/
https://www.ncbi.nlm.nih.gov/pubmed/27176711
http://dx.doi.org/10.1371/journal.pone.0155537
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