Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530
Abstract Dimethylsulfoniopropionate (DMSP) is widespread in the oceans, and its biological metabolite, dimethyl sulfide (DMS), plays an important role in the atmosphere. The Antarctic region has become a hotspot in DMS studies due to the high spatial and temporal variability in DMS(P) concentration,...
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crwiley:10.1002/jobm.202000032 2023-10-29T02:31:52+01:00 Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 Wang, Wenyu Qu, Changfeng Wang, Xixi Gao, Xuxu Zhang, Honghai Miao, Jinlai Natural Science Foundation of Shandong Province China Ocean Mineral Resources Research and Development Association 2020 http://dx.doi.org/10.1002/jobm.202000032 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjobm.202000032 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jobm.202000032 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of Basic Microbiology volume 60, issue 7, page 639-648 ISSN 0233-111X 1521-4028 Applied Microbiology and Biotechnology General Medicine journal-article 2020 crwiley https://doi.org/10.1002/jobm.202000032 2023-10-02T16:29:15Z Abstract Dimethylsulfoniopropionate (DMSP) is widespread in the oceans, and its biological metabolite, dimethyl sulfide (DMS), plays an important role in the atmosphere. The Antarctic region has become a hotspot in DMS studies due to the high spatial and temporal variability in DMS(P) concentration, but the level of bacterial DMS production remains unclear. In this study, a bacterium isolated from Antarctic floating ice, Rhodococcus sp. NJ‐530, was found to metabolize DMSP into DMS, and the rate of DMS production was measured as 3.96 pmol·mg protein −1 ·h −1 . Rhodococcus sp. NJ‐530 had a DddD‐ Rh enzyme containing two CaiB domains, which belonged to the CoA‐transferase III superfamily. However, the DddD‐ Rh had a molecular weight of 73.21 kDa, which was very different from previously characterized DddD enzymes in sequence and evolution. In vitro assays showed that DddD‐ Rh was functional in the presence of acetyl‐CoA. This was the first functional DddD from Gram‐positive Actinobacteria. Moreover, a quantitative real‐time polymerase chain reaction revealed that high temperature facilitated the expression of dddD ‐ Rh , and changes of salinity had little effect on it. This study adds new evidence to the bacterial DMS production in the Southern Ocean and provides a basis for investigating the metabolic mechanism of DMSP in extreme environments. Article in Journal/Newspaper Antarc* Antarctic Southern Ocean Wiley Online Library (via Crossref) Journal of Basic Microbiology 60 7 639 648 |
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Wiley Online Library (via Crossref) |
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language |
English |
topic |
Applied Microbiology and Biotechnology General Medicine |
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Applied Microbiology and Biotechnology General Medicine Wang, Wenyu Qu, Changfeng Wang, Xixi Gao, Xuxu Zhang, Honghai Miao, Jinlai Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 |
topic_facet |
Applied Microbiology and Biotechnology General Medicine |
description |
Abstract Dimethylsulfoniopropionate (DMSP) is widespread in the oceans, and its biological metabolite, dimethyl sulfide (DMS), plays an important role in the atmosphere. The Antarctic region has become a hotspot in DMS studies due to the high spatial and temporal variability in DMS(P) concentration, but the level of bacterial DMS production remains unclear. In this study, a bacterium isolated from Antarctic floating ice, Rhodococcus sp. NJ‐530, was found to metabolize DMSP into DMS, and the rate of DMS production was measured as 3.96 pmol·mg protein −1 ·h −1 . Rhodococcus sp. NJ‐530 had a DddD‐ Rh enzyme containing two CaiB domains, which belonged to the CoA‐transferase III superfamily. However, the DddD‐ Rh had a molecular weight of 73.21 kDa, which was very different from previously characterized DddD enzymes in sequence and evolution. In vitro assays showed that DddD‐ Rh was functional in the presence of acetyl‐CoA. This was the first functional DddD from Gram‐positive Actinobacteria. Moreover, a quantitative real‐time polymerase chain reaction revealed that high temperature facilitated the expression of dddD ‐ Rh , and changes of salinity had little effect on it. This study adds new evidence to the bacterial DMS production in the Southern Ocean and provides a basis for investigating the metabolic mechanism of DMSP in extreme environments. |
author2 |
Natural Science Foundation of Shandong Province China Ocean Mineral Resources Research and Development Association |
format |
Article in Journal/Newspaper |
author |
Wang, Wenyu Qu, Changfeng Wang, Xixi Gao, Xuxu Zhang, Honghai Miao, Jinlai |
author_facet |
Wang, Wenyu Qu, Changfeng Wang, Xixi Gao, Xuxu Zhang, Honghai Miao, Jinlai |
author_sort |
Wang, Wenyu |
title |
Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 |
title_short |
Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 |
title_full |
Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 |
title_fullStr |
Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 |
title_full_unstemmed |
Identification of a functional dddD ‐ Rh for dimethyl sulfide production in the Antarctic Rhodococcus sp. NJ‐530 |
title_sort |
identification of a functional dddd ‐ rh for dimethyl sulfide production in the antarctic rhodococcus sp. nj‐530 |
publisher |
Wiley |
publishDate |
2020 |
url |
http://dx.doi.org/10.1002/jobm.202000032 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjobm.202000032 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jobm.202000032 |
genre |
Antarc* Antarctic Southern Ocean |
genre_facet |
Antarc* Antarctic Southern Ocean |
op_source |
Journal of Basic Microbiology volume 60, issue 7, page 639-648 ISSN 0233-111X 1521-4028 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/jobm.202000032 |
container_title |
Journal of Basic Microbiology |
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60 |
container_issue |
7 |
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639 |
op_container_end_page |
648 |
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1781052711869874176 |