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Li, Chun-Yang, Crack, Jason C., Newton-Payne, Simone, Murphy, Andrew R. J., Chen, Xiu-Lan, Pinchbeck, Benjamin J., Zhou, Shun, Williams, Beth T. 
ORCID: https://orcid.org/0000-0002-8594-1269, Peng, Ming, Zhang, Xiao-Hua, Chen, Yin, Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Todd, Jonathan D. and Zhang, Yu-Zhong
(2022)
Mechanistic insights into the key marine dimethylsulfoniopropionate synthesis enzyme DsyB/DSYB.
mLife, 1 (2).
pp. 114-130.
ISSN 2770-100X
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Abstract
Marine algae and bacteria produce approximately eight billion tonnes of the organosulfur molecule dimethylsulfoniopropionate (DMSP) in Earth's surface oceans annually. DMSP is an antistress compound and, once released into the environment, a major nutrient, signaling molecule, and source of climate-active gases. The methionine transamination pathway for DMSP synthesis is used by most known DMSP-producing algae and bacteria. The S-directed S-adenosylmethionine (SAM)-dependent 4-methylthio-2-hydroxybutyrate (MTHB) S-methyltransferase, encoded by the dsyB/DSYB gene, is the key enzyme of this pathway, generating S-adenosylhomocysteine (SAH) and 4-dimethylsulfonio-2-hydroxybutyrate (DMSHB). DsyB/DSYB, present in most haptophyte and dinoflagellate algae with the highest known intracellular DMSP concentrations, is shown to be far more abundant and transcribed in marine environments than any other known S-methyltransferase gene in DMSP synthesis pathways. Furthermore, we demonstrate in vitro activity of the bacterial DsyB enzyme from Nisaea denitrificans and provide its crystal structure in complex with SAM and SAH-MTHB, which together provide the first important mechanistic insights into a DMSP synthesis enzyme. Structural and mutational analyses imply that DsyB adopts a proximity and desolvation mechanism for the methyl transfer reaction. Sequence analysis suggests that this mechanism may be common to all bacterial DsyB enzymes and also, importantly, eukaryotic DSYB enzymes from e.g., algae that are the major DMSP producers in Earth's surface oceans.
| Item Type: | Article |
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| Additional Information: | ACKNOWLEDGMENTS: We thank the staff from BL18U1&BL19U1 beamlines of the National Facility for Protein Sciences Shanghai (NFPS) and Shanghai Synchrotron Radiation Facility, for assistance during data collection. This work was supported by: the National Science Foundation of China (grants 91851205, 42076229, 31961133016), the National Key Research and Development Program of China (2021YFA0909600), the Fundamental Research Funds for the Central Universities (202172002, 202041011), the Major Scientific and Technological Innovation Project (MSTIP) of Shandong Province (2019JZZY010817), the Program of Shandong for Taishan Scholars (tspd20181203), the grant of Laboratory for Marine Biology and Biotechnology (OF2019NO02), Pilot National Laboratory for Marine Science and Technology (Qingdao), the United Kingdom’s Natural and Environmental Research Council (NERC, NE/P012671/1 and NE/N002385/1), and the United Kingdom’s Biotechnology and Biological Sciences Research Council (BBSRC, BB/P006140/1). |
| Uncontrolled Keywords: | dmsp synthesis,marine sulfur cycling,s-methyltarnsferases,marine sulfur cycle,catalytic mechanism,s-methyltransferase,microbiology,sdg 14 - life below water,sdg 13 - climate action ,/dk/atira/pure/subjectarea/asjc/2400/2404 |
| Faculty \ School: | Faculty of Science > School of Chemistry (former - to 2024) Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Molecular Microbiology |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 24 May 2022 16:00 |
| Last Modified: | 05 Nov 2024 00:48 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/85139 |
| DOI: | 10.1002/mlf2.12030 |
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