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Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis
Biotin protein ligase (BPL) is widespread in the three domains of the life. The paradigm BPL is the Escherichia coli BirA protein, which also functions as a repressor for the biotin biosynthesis pathway. Here we report that Lactococcus lactis possesses two different orthologues of birA (birA1(_LL) a...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4861984/ https://www.ncbi.nlm.nih.gov/pubmed/27161258 http://dx.doi.org/10.1038/srep25680 |
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author | Zhang, Huimin Wang, Qingjing Fisher, Derek J. Cai, Mingzhu Chakravartty, Vandana Ye, Huiyan Li, Ping Solbiati, Jose O. Feng, Youjun |
author_facet | Zhang, Huimin Wang, Qingjing Fisher, Derek J. Cai, Mingzhu Chakravartty, Vandana Ye, Huiyan Li, Ping Solbiati, Jose O. Feng, Youjun |
author_sort | Zhang, Huimin |
collection | PubMed |
description | Biotin protein ligase (BPL) is widespread in the three domains of the life. The paradigm BPL is the Escherichia coli BirA protein, which also functions as a repressor for the biotin biosynthesis pathway. Here we report that Lactococcus lactis possesses two different orthologues of birA (birA1(_LL) and birA2(_LL)). Unlike the scenario in E. coli, L. lactis appears to be auxotrophic for biotin in that it lacks a full biotin biosynthesis pathway. In contrast, it retains two biotin transporter-encoding genes (bioY1(_LL) and bioY2(_LL)), suggesting the use of a scavenging strategy to obtain biotin from the environment. The in vivo function of the two L. lactis birA genes was judged by their abilities to complement the conditional lethal E. coli birA mutant. Thin-layer chromatography and mass spectroscopy assays demonstrated that these two recombinant BirA proteins catalyze the biotinylation reaction of the acceptor biotin carboxyl carrier protein (BCCP), through the expected biotinoyl-AMP intermediate. Gel shift assays were used to characterize bioY1(_LL) and BirA1(_LL). We also determined the ability to uptake (3)H-biotin by L. lactis. Taken together, our results deciphered a unique biotin scavenging pathway with redundant genes present in the probiotic bacterium L. lactis. |
format | Online Article Text |
id | pubmed-4861984 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48619842016-05-23 Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis Zhang, Huimin Wang, Qingjing Fisher, Derek J. Cai, Mingzhu Chakravartty, Vandana Ye, Huiyan Li, Ping Solbiati, Jose O. Feng, Youjun Sci Rep Article Biotin protein ligase (BPL) is widespread in the three domains of the life. The paradigm BPL is the Escherichia coli BirA protein, which also functions as a repressor for the biotin biosynthesis pathway. Here we report that Lactococcus lactis possesses two different orthologues of birA (birA1(_LL) and birA2(_LL)). Unlike the scenario in E. coli, L. lactis appears to be auxotrophic for biotin in that it lacks a full biotin biosynthesis pathway. In contrast, it retains two biotin transporter-encoding genes (bioY1(_LL) and bioY2(_LL)), suggesting the use of a scavenging strategy to obtain biotin from the environment. The in vivo function of the two L. lactis birA genes was judged by their abilities to complement the conditional lethal E. coli birA mutant. Thin-layer chromatography and mass spectroscopy assays demonstrated that these two recombinant BirA proteins catalyze the biotinylation reaction of the acceptor biotin carboxyl carrier protein (BCCP), through the expected biotinoyl-AMP intermediate. Gel shift assays were used to characterize bioY1(_LL) and BirA1(_LL). We also determined the ability to uptake (3)H-biotin by L. lactis. Taken together, our results deciphered a unique biotin scavenging pathway with redundant genes present in the probiotic bacterium L. lactis. Nature Publishing Group 2016-05-10 /pmc/articles/PMC4861984/ /pubmed/27161258 http://dx.doi.org/10.1038/srep25680 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Zhang, Huimin Wang, Qingjing Fisher, Derek J. Cai, Mingzhu Chakravartty, Vandana Ye, Huiyan Li, Ping Solbiati, Jose O. Feng, Youjun Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis |
title | Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis |
title_full | Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis |
title_fullStr | Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis |
title_full_unstemmed | Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis |
title_short | Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis |
title_sort | deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium lactococcus lactis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4861984/ https://www.ncbi.nlm.nih.gov/pubmed/27161258 http://dx.doi.org/10.1038/srep25680 |
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