Advanced search
2 files | 6.00 MB Add to list

Structural and biochemical characterization of SmoPG1, an exo-polygalacturonase from Selaginella moellendorffii

Author
Organization
Abstract
Polygalacturonases (PGs) can modulate chemistry and mechanical properties of the plant cell wall through the degradation of pectins, one of its major constituents. PGs are largely used in food, beverage, textile, and paper industries to increase processes' performances. To improve the use of PGs, knowledge of their biochemical, structural and functional features is of prime importance. Our study aims at characterizing SmoPG1, a polygalacturonase from Selaginella moellendorffii, that belongs to the lycophytes. Transcription data showed that SmoPG1 was mainly expressed in S. moellendorffii shoots while phylogenetic analyses suggested that SmoPG1 is an exo-PG, which was confirmed by the biochemical characterization following its expression in heterologous system. Indeed, LC-MS/MS oligoprofiling using various pectic substrates identified galacturonic acid (GalA) as the main hydrolysis product. We found that SmoPG1 was most active on polygalacturonic acid (PGA) at pH 5, and that its activity could be modulated by different cations (Ca2+, Cu2+, Fe2+, Mg2+, Mn2+, Na2+, Zn2+). In addition, SmoPG1 was inhibited by green tea catechins, including (-)-epigallocatechin-3-gallate (EGCG). Docking analyses and MD simulations showed in detail amino acids responsible for the SmoPG1-EGCG interaction. Considering its expression yield and activity, SmoPG1 appears as a prime candidate for the industrial production of GalA.
Keywords
Pectins, Plant cell wall, Polygalacturonases, Selaginella moellendorffii, ENDO-POLYGALACTURONASE, EXOPOLYGALACTURONASE, PURIFICATION, EXPRESSION, DYNAMICS, INSIGHTS, PLANT, IDENTIFICATION, SPECIFICITY, PECTINASES

Downloads

  • Carton et al manuscript - Revision (clean version).pdf
    • full text (Accepted manuscript)
    • |
    • open access
    • |
    • PDF
    • |
    • 1.73 MB
  • (...).pdf
    • full text (Published version)
    • |
    • UGent only
    • |
    • PDF
    • |
    • 4.27 MB

Citation

Please use this url to cite or link to this publication:

MLA
Carton, Camille, et al. “Structural and Biochemical Characterization of SmoPG1, an Exo-Polygalacturonase from Selaginella Moellendorffii.” INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, vol. 269, no. 2, 2024, doi:10.1016/j.ijbiomac.2024.131918.
APA
Carton, C., Safran, J., Lemaire, A., Domon, J.-M., Poelmans, W., Beeckman, T., … Pau-Roblot, C. (2024). Structural and biochemical characterization of SmoPG1, an exo-polygalacturonase from Selaginella moellendorffii. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 269(2). https://doi.org/10.1016/j.ijbiomac.2024.131918
Chicago author-date
Carton, Camille, Josip Safran, Adrien Lemaire, Jean-Marc Domon, Ward Poelmans, Tom Beeckman, Francisco Ramos-Martín, et al. 2024. “Structural and Biochemical Characterization of SmoPG1, an Exo-Polygalacturonase from Selaginella Moellendorffii.” INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 269 (2). https://doi.org/10.1016/j.ijbiomac.2024.131918.
Chicago author-date (all authors)
Carton, Camille, Josip Safran, Adrien Lemaire, Jean-Marc Domon, Ward Poelmans, Tom Beeckman, Francisco Ramos-Martín, Viviane Antonietti, Pascal Sonnet, Anissa Lounès-Hadj Sahraoui, Valérie Lefebvre, Jérôme Pelloux, and Corinne Pau-Roblot. 2024. “Structural and Biochemical Characterization of SmoPG1, an Exo-Polygalacturonase from Selaginella Moellendorffii.” INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 269 (2). doi:10.1016/j.ijbiomac.2024.131918.
Vancouver
1.
Carton C, Safran J, Lemaire A, Domon J-M, Poelmans W, Beeckman T, et al. Structural and biochemical characterization of SmoPG1, an exo-polygalacturonase from Selaginella moellendorffii. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. 2024;269(2).
IEEE
[1]
C. Carton et al., “Structural and biochemical characterization of SmoPG1, an exo-polygalacturonase from Selaginella moellendorffii,” INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, vol. 269, no. 2, 2024.
@article{01HXBHW49CN4Q0HNCX901R7MCG,
  abstract     = {{Polygalacturonases (PGs) can modulate chemistry and mechanical properties of the plant cell wall through the degradation of pectins, one of its major constituents. PGs are largely used in food, beverage, textile, and paper industries to increase processes' performances. To improve the use of PGs, knowledge of their biochemical, structural and functional features is of prime importance. Our study aims at characterizing SmoPG1, a polygalacturonase from Selaginella moellendorffii, that belongs to the lycophytes. Transcription data showed that SmoPG1 was mainly expressed in S. moellendorffii shoots while phylogenetic analyses suggested that SmoPG1 is an exo-PG, which was confirmed by the biochemical characterization following its expression in heterologous system. Indeed, LC-MS/MS oligoprofiling using various pectic substrates identified galacturonic acid (GalA) as the main hydrolysis product. We found that SmoPG1 was most active on polygalacturonic acid (PGA) at pH 5, and that its activity could be modulated by different cations (Ca2+, Cu2+, Fe2+, Mg2+, Mn2+, Na2+, Zn2+). In addition, SmoPG1 was inhibited by green tea catechins, including (-)-epigallocatechin-3-gallate (EGCG). Docking analyses and MD simulations showed in detail amino acids responsible for the SmoPG1-EGCG interaction. Considering its expression yield and activity, SmoPG1 appears as a prime candidate for the industrial production of GalA.}},
  articleno    = {{131918}},
  author       = {{Carton, Camille and Safran, Josip and Lemaire, Adrien and Domon, Jean-Marc and Poelmans, Ward and Beeckman, Tom and Ramos-Martín, Francisco and Antonietti, Viviane and Sonnet, Pascal and Sahraoui, Anissa Lounès-Hadj and Lefebvre, Valérie and Pelloux, Jérôme and Pau-Roblot, Corinne}},
  issn         = {{0141-8130}},
  journal      = {{INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES}},
  keywords     = {{Pectins,Plant cell wall,Polygalacturonases,Selaginella moellendorffii,ENDO-POLYGALACTURONASE,EXOPOLYGALACTURONASE,PURIFICATION,EXPRESSION,DYNAMICS,INSIGHTS,PLANT,IDENTIFICATION,SPECIFICITY,PECTINASES}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{11}},
  title        = {{Structural and biochemical characterization of SmoPG1, an exo-polygalacturonase from Selaginella moellendorffii}},
  url          = {{http://doi.org/10.1016/j.ijbiomac.2024.131918}},
  volume       = {{269}},
  year         = {{2024}},
}

Altmetric
View in Altmetric
Web of Science
Times cited: