Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgaeCitation formats

  • External authors:
  • Ben A Wagstaff
  • Martin Rejzek
  • Sakonwan Kuhaudomlarp
  • Lionel Hill
  • Ilaria Mascia
  • Sergey A Nepogodiev
  • Helge C Dorfmueller

Standard

Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae. / Wagstaff, Ben A; Rejzek, Martin; Kuhaudomlarp, Sakonwan; Hill, Lionel; Mascia, Ilaria; Nepogodiev, Sergey A; Dorfmueller, Helge C; Field, Robert A.

In: Journal of Biological Chemistry, Vol. 294, No. 23, 07.06.2019, p. 9172-9185.

Research output: Contribution to journalArticlepeer-review

Harvard

Wagstaff, BA, Rejzek, M, Kuhaudomlarp, S, Hill, L, Mascia, I, Nepogodiev, SA, Dorfmueller, HC & Field, RA 2019, 'Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae', Journal of Biological Chemistry, vol. 294, no. 23, pp. 9172-9185. https://doi.org/10.1074/jbc.RA118.006440

APA

Wagstaff, B. A., Rejzek, M., Kuhaudomlarp, S., Hill, L., Mascia, I., Nepogodiev, S. A., Dorfmueller, H. C., & Field, R. A. (2019). Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae. Journal of Biological Chemistry, 294(23), 9172-9185. https://doi.org/10.1074/jbc.RA118.006440

Vancouver

Wagstaff BA, Rejzek M, Kuhaudomlarp S, Hill L, Mascia I, Nepogodiev SA et al. Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae. Journal of Biological Chemistry. 2019 Jun 7;294(23):9172-9185. https://doi.org/10.1074/jbc.RA118.006440

Author

Wagstaff, Ben A ; Rejzek, Martin ; Kuhaudomlarp, Sakonwan ; Hill, Lionel ; Mascia, Ilaria ; Nepogodiev, Sergey A ; Dorfmueller, Helge C ; Field, Robert A. / Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae. In: Journal of Biological Chemistry. 2019 ; Vol. 294, No. 23. pp. 9172-9185.

Bibtex

@article{ca7f9b3b27754a73aa6cc9df10ffb2ba,
title = "Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae",
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-β-l-rhamnose (UDP-β-l-Rha) or thymidine 5'-diphospho-β-l-rhamnose (TDP-β-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-β-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 β-l-Rha (NDP-β-l-Rha) pathways among algae.",
keywords = "Algal Proteins/genetics, Carbohydrate Epimerases/classification, Haptophyta/metabolism, Phylogeny, Plastids/metabolism, Recombinant Fusion Proteins/genetics, Rhamnose/biosynthesis, Symbiosis",
author = "Wagstaff, {Ben A} and Martin Rejzek and Sakonwan Kuhaudomlarp and Lionel Hill and Ilaria Mascia and Nepogodiev, {Sergey A} and Dorfmueller, {Helge C} and Field, {Robert A}",
note = "{\textcopyright} 2019 Wagstaff et al.",
year = "2019",
month = jun,
day = "7",
doi = "10.1074/jbc.RA118.006440",
language = "English",
volume = "294",
pages = "9172--9185",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "23",

}

RIS

TY - JOUR

T1 - Discovery of an RmlC/D fusion protein in the microalga Prymnesium parvum and its implications for NDP-β-l-rhamnose biosynthesis in microalgae

AU - Wagstaff, Ben A

AU - Rejzek, Martin

AU - Kuhaudomlarp, Sakonwan

AU - Hill, Lionel

AU - Mascia, Ilaria

AU - Nepogodiev, Sergey A

AU - Dorfmueller, Helge C

AU - Field, Robert A

N1 - © 2019 Wagstaff et al.

PY - 2019/6/7

Y1 - 2019/6/7

N2 - 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-β-l-rhamnose (UDP-β-l-Rha) or thymidine 5'-diphospho-β-l-rhamnose (TDP-β-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-β-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 β-l-Rha (NDP-β-l-Rha) pathways among algae.

AB - 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-β-l-rhamnose (UDP-β-l-Rha) or thymidine 5'-diphospho-β-l-rhamnose (TDP-β-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-β-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 β-l-Rha (NDP-β-l-Rha) pathways among algae.

KW - Algal Proteins/genetics

KW - Carbohydrate Epimerases/classification

KW - Haptophyta/metabolism

KW - Phylogeny

KW - Plastids/metabolism

KW - Recombinant Fusion Proteins/genetics

KW - Rhamnose/biosynthesis

KW - Symbiosis

U2 - 10.1074/jbc.RA118.006440

DO - 10.1074/jbc.RA118.006440

M3 - Article

C2 - 31010825

VL - 294

SP - 9172

EP - 9185

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 23

ER -