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Journal articles
Analysis of LuPME3, a pectin methylesterase from Linum usitatissimum, revealed a variability in PME proteolytic maturation
Abstract : Pectin methylesterase (PME) catalyzes the de-methylesterification of pectin in plant cell walls during cell elongation.1
Pectins are mainly composed of a(1, 4)-D-galacturonosyl acid units that are synthesized in a methylesterified form in the
Golgi apparatus to prevent any interaction with Ca2+ ions during their intracellular transport.2 The highly methylesterified
pectins are then secreted into the apoplasm3 and subsequently de-methylesterified in muro by PMEs. This can either
induce the formation of pectin gels through the Ca2+ crosslinking of neighboring non-methylesterified chains or create
substrates for pectin-degrading enzymes such as polygalacturonases and pectate lyases for the initiation of cell wall
loosening.4 PMEs belong to a large multigene family. Sixt-six PME-related genes are predicted in the Arabidopsis
genome.1 Among them, we have recently shown that AtPME3 (At3g14310), a major basic PME isoform in A. thaliana, is
ubiquitously expressed in vascular tissues and play a role in adventitious rooting.5 In flax (Linum usitatissimum), three
genes encoding PMEs have been sequenced so far, including LuPME3, the ortholog of AtPME3. Analysis of the LuPME3
isoform brings new insights into the processing of these proteins.
https://hal-normandie-univ.archives-ouvertes.fr/hal-01848279
Contributor : Arnaud Lehner <>
Submitted on : Tuesday, July 24, 2018 - 2:36:02 PM
Last modification on : Thursday, July 2, 2020 - 3:28:51 AM
Contributor : Arnaud Lehner <>
Submitted on : Tuesday, July 24, 2018 - 2:36:02 PM
Last modification on : Thursday, July 2, 2020 - 3:28:51 AM
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