Tools
Tools
Wagstaff, Ben A., Rejzek, Martin, Kuhaudomlarp, Sakonwan, Hill, Lionel, Mascia, Ilaria, Nepogodiev, Sergey A., Dorfmueller, Helge C. and Field, Robert A. 
ORCID: https://orcid.org/0000-0001-8574-0275
(2019)
Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-L-rhamnose biosynthesis in microalgae.
Journal of Biological Chemistry, 294 (23).
pp. 9172-9185.
ISSN 0021-9258
Abstract
The 6-deoxy sugar L-rhamnose (L-Rha) is found widely in plant and microbial polysaccharides and natural products. The importance of this and related compounds in host–pathogen interactions often means that L-Rha plays an essential role in many organisms. L-Rha is most commonly biosynthesized as the activated sugar nucleotide uridine 5-diphospho-L-rhamnose (UDP-L-Rha) or thymidine 5-diphospho-L-rhamnose (TDP-L-Rha). Enzymes involved in the biosynthesis of these sugar nucleotides have been studied in some detail in bacteria and plants, but the activated form of L-Rha and the corresponding biosynthetic enzymes have yet to be explored in algae. Here, using sugar-nucleotide profiling in two representative algae, Euglena gracilis and the toxin-producing microalga Prymnesium parvum, we show that levels of UDP- and TDP-activated L-Rha differ significantly between these two algal species. Using bioinformatics and biochemical methods, we identified and characterized a fusion of the RmlC and RmlD proteins, two bacteria-like enzymes involved in TDP-L-Rha biosynthesis, from P. parvum. Using this new sequence and also others, we explored L-Rha biosynthesis among algae, finding that although most algae contain sequences orthologous to plant-like L-Rha biosynthesis machineries, instances of the RmlC-RmlD fusion protein identified here exist across the Haptophyta and Gymnodiniaceae families of microalgae. On the basis of these findings, we propose potential routes for the evolution of nucleoside diphosphate -L-Rha (NDP-L-Rha) pathways among algae.
| Item Type: | Article |
|---|---|
| Additional Information: | Funding Information: This work was funded by the UK Biotechnological and Biological Sciences Research Council (BBSRC) Institute Strategic Programme Grant “Molecules from Nature—Products and Pathways” BBS/E/J/000PR9790 and the John Innes Foundation. This work was also supported by Grant 109357/Z/15/Z from Wellcome Trust and Royal Society (to H. C. D.).” The authors declare that they have no conflicts of interest with the contents of this article. We thank Dr. Gill Malin for useful discussions on algal taxonomy and Dr. Michael Rugen for advice on heterologous expression. We thank Prof. Jim Naismith for provision of the S. enterica Typhimurium RmlB clone and Prof. Michela Tonetti for provision of the ATCV-1 UGD clone. Funding Information: This work was funded by the UK Biotechnological and Biological Sciences Research Council (BBSRC) Institute Strategic Programme Grant “Molecules from Nature—Products and Pathways” BBS/E/J/000PR9790 and the John Innes Foundation. This work was also supported by Grant 109357/Z/15/Z from Wellcome Trust and Royal Society (to H. C. D.).” The authors declare that they have no conflicts of interest with the contents of this article. Publisher Copyright: © 2019 Wagstaff et al. |
| Uncontrolled Keywords: | biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 02 Sep 2024 15:30 |
| Last Modified: | 25 Sep 2024 18:05 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96447 |
| DOI: | 10.1074/jbc.RA118.006440 |
Actions (login required)
 |
View Item |