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Mutation of AtPME2, a pH-dependent pectin methylesterase, affects cell wall structure and hypocotyl elongation

Ludivine Hocq, Olivier Habrylo, Fabien Sénéchal, Aline Voxeur, Corinne Pau-Roblot, Josip Safran, Françoise Fournet, Solène Bassard, Virginie Battu, Hervé Demailly, et al.
(2024) PLANT AND CELL PHYSIOLOGY. 65(2). p.301-318
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Abstract
Pectin methylesterases (PMEs) modify homogalacturonan’s chemistry and play a key role in regulating primary cell wall mechanical properties. Here, we report on Arabidopsis AtPME2, which we found to be highly expressed during lateral root emergence and dark-grown hypocotyl elongation. We showed that dark-grown hypocotyl elongation was reduced in knock-out mutant lines as compared to the control. The latter was related to the decreased total PME activity as well as increased stiffness of the cell wall in the apical part of the hypocotyl. To relate phenotypic analyses to the biochemical specificity of the enzyme, we produced the mature active enzyme using heterologous expression in Pichia pastoris and characterized it through the use of a generic plant PME antiserum. AtPME2 is more active at neutral compared to acidic pH, on pectins with a degree of 55–70% methylesterification. We further showed that the mode of action of AtPME2 can vary according to pH, from high processivity (at pH8) to low processivity (at pH5), and relate these observations to the differences in electrostatic potential of the protein. Our study brings insights into how the pH-dependent regulation by PME activity could affect the pectin structure and associated cell wall mechanical properties.
Keywords
Arabidopsis thaliana, Cell wall, Hypocotyl, Pectin methylesterase, Processivity, Roots, METHYL ESTERASE, MODEL HOMOGALACTURONAN, PICHIA-PASTORIS, ACTION PATTERNS, ENZYME MODE, ROOT, EXPRESSION, INSIGHTS, PROTEIN, GROWTH

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Citation

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MLA
Hocq, Ludivine, et al. “Mutation of AtPME2, a PH-Dependent Pectin Methylesterase, Affects Cell Wall Structure and Hypocotyl Elongation.” PLANT AND CELL PHYSIOLOGY, vol. 65, no. 2, 2024, pp. 301–18, doi:10.1093/pcp/pcad154.
APA
Hocq, L., Habrylo, O., Sénéchal, F., Voxeur, A., Pau-Roblot, C., Safran, J., … Lefebvre, V. (2024). Mutation of AtPME2, a pH-dependent pectin methylesterase, affects cell wall structure and hypocotyl elongation. PLANT AND CELL PHYSIOLOGY, 65(2), 301–318. https://doi.org/10.1093/pcp/pcad154
Chicago author-date
Hocq, Ludivine, Olivier Habrylo, Fabien Sénéchal, Aline Voxeur, Corinne Pau-Roblot, Josip Safran, Françoise Fournet, et al. 2024. “Mutation of AtPME2, a PH-Dependent Pectin Methylesterase, Affects Cell Wall Structure and Hypocotyl Elongation.” PLANT AND CELL PHYSIOLOGY 65 (2): 301–18. https://doi.org/10.1093/pcp/pcad154.
Chicago author-date (all authors)
Hocq, Ludivine, Olivier Habrylo, Fabien Sénéchal, Aline Voxeur, Corinne Pau-Roblot, Josip Safran, Françoise Fournet, Solène Bassard, Virginie Battu, Hervé Demailly, José C. Tovar, Serge Pilard, Paulo Marcelo, Brett J. Savary, Davide Mercadante, Maria Njo, Tom Beeckman, Arezki Boudaoud, Laurent Gutierrez, Jérôme Pelloux, and Valérie Lefebvre. 2024. “Mutation of AtPME2, a PH-Dependent Pectin Methylesterase, Affects Cell Wall Structure and Hypocotyl Elongation.” PLANT AND CELL PHYSIOLOGY 65 (2): 301–318. doi:10.1093/pcp/pcad154.
Vancouver
1.
Hocq L, Habrylo O, Sénéchal F, Voxeur A, Pau-Roblot C, Safran J, et al. Mutation of AtPME2, a pH-dependent pectin methylesterase, affects cell wall structure and hypocotyl elongation. PLANT AND CELL PHYSIOLOGY. 2024;65(2):301–18.
IEEE
[1]
L. Hocq et al., “Mutation of AtPME2, a pH-dependent pectin methylesterase, affects cell wall structure and hypocotyl elongation,” PLANT AND CELL PHYSIOLOGY, vol. 65, no. 2, pp. 301–318, 2024.
@article{01HMR7VDZTVHHPVEWX9EY7GX8G,
  abstract     = {{Pectin methylesterases (PMEs) modify homogalacturonan’s chemistry and play a key role in regulating primary cell wall mechanical properties. Here, we report on Arabidopsis AtPME2, which we found to be highly expressed during lateral root emergence and dark-grown hypocotyl elongation. We showed that dark-grown hypocotyl elongation was reduced in knock-out mutant lines as compared to the control. The latter was related to the decreased total PME activity as well as increased stiffness of the cell wall in the apical part of the hypocotyl. To relate phenotypic analyses to the biochemical specificity of the enzyme, we produced the mature active enzyme using heterologous expression in Pichia pastoris and characterized it through the use of a generic plant PME antiserum. AtPME2 is more active at neutral compared to acidic pH, on pectins with a degree of 55–70% methylesterification. We further showed that the mode of action of AtPME2 can vary according to pH, from high processivity (at pH8) to low processivity (at pH5), and relate these observations to the differences in electrostatic potential of the protein. Our study brings insights into how the pH-dependent regulation by PME activity could affect the pectin structure and associated cell wall mechanical properties.}},
  author       = {{Hocq, Ludivine and Habrylo, Olivier and Sénéchal, Fabien and Voxeur, Aline and Pau-Roblot, Corinne and Safran, Josip and Fournet, Françoise and Bassard, Solène and Battu, Virginie and Demailly, Hervé and Tovar, José C. and Pilard, Serge and Marcelo, Paulo and Savary, Brett J. and Mercadante, Davide and Njo, Maria and Beeckman, Tom and Boudaoud, Arezki and Gutierrez, Laurent and Pelloux, Jérôme and Lefebvre, Valérie}},
  issn         = {{0032-0781}},
  journal      = {{PLANT AND CELL PHYSIOLOGY}},
  keywords     = {{Arabidopsis thaliana,Cell wall,Hypocotyl,Pectin methylesterase,Processivity,Roots,METHYL ESTERASE,MODEL HOMOGALACTURONAN,PICHIA-PASTORIS,ACTION PATTERNS,ENZYME MODE,ROOT,EXPRESSION,INSIGHTS,PROTEIN,GROWTH}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{301--318}},
  title        = {{Mutation of AtPME2, a pH-dependent pectin methylesterase, affects cell wall structure and hypocotyl elongation}},
  url          = {{http://doi.org/10.1093/pcp/pcad154}},
  volume       = {{65}},
  year         = {{2024}},
}
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