Cutin:cutin-acid endo-transacylase (CCT), a cuticleremodelling enzyme activity in the plant epidermis
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Cutin:cutin-acid endo-transacylase (CCT), a cuticleremodelling enzyme activity in the plant epidermis. / Xin, Anzhou; Fei, Yue; Molnar, Attila; Fry, Stephen C.
In: Biochemical Journal, Vol. 478, No. 4, 02.2021, p. 777-798.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Cutin:cutin-acid endo-transacylase (CCT), a cuticleremodelling enzyme activity in the plant epidermis
AU - Xin, Anzhou
AU - Fei, Yue
AU - Molnar, Attila
AU - Fry, Stephen C.
N1 - Funding Information: This work was enabled by AX’s family with additional support from the U.K. Biotechnology and Biological Sciences Research Council (BBSRC; BB/N002458/1). Publisher Copyright: © 2021 Portland Press Ltd. All rights reserved.
PY - 2021/2
Y1 - 2021/2
N2 - Cutin is a polyester matrix mainly composed of hydroxy-fatty acids that occurs in the cuticles of shoots and root-caps. The cuticle, of which cutin is a major component, protects the plant from biotic and abiotic stresses, and cutin has been postulated to constrain organ expansion. We propose that, to allow cutin restructuring, ester bonds in this net-like polymer can be transiently cleaved and then re-formed (transacylation). Here, using pea epicotyl epidermis as the main model, we first detected a cutin:cutin-fatty acid endo-transacylase (CCT) activity. In-situ assays used endogenous cutin as the donor substrate for endogenous enzymes; the exogenous acceptor substrate was a radiolabelled monomeric cutin-acid, 16-hydroxy-[3H]hexadecanoic acid (HHA). High-molecularweight cutin became ester-bonded to intact [3H]HHA molecules, which thereby became unextractable except by ester-hydrolysing alkalis. In-situ CCT activity correlated with growth rate in Hylotelephium leaves and tomato fruits, suggesting a role in loosening the outer epidermal wall during organ growth. The only well-defined cutin transacylase in the apoplast, CUS1 (a tomato cutin synthase), when produced in transgenic tobacco, lacked CCT activity. This finding provides a reference for future CCT protein identification, which can adopt our sensitive enzyme assay to screen other CUS1-related enzymes.
AB - Cutin is a polyester matrix mainly composed of hydroxy-fatty acids that occurs in the cuticles of shoots and root-caps. The cuticle, of which cutin is a major component, protects the plant from biotic and abiotic stresses, and cutin has been postulated to constrain organ expansion. We propose that, to allow cutin restructuring, ester bonds in this net-like polymer can be transiently cleaved and then re-formed (transacylation). Here, using pea epicotyl epidermis as the main model, we first detected a cutin:cutin-fatty acid endo-transacylase (CCT) activity. In-situ assays used endogenous cutin as the donor substrate for endogenous enzymes; the exogenous acceptor substrate was a radiolabelled monomeric cutin-acid, 16-hydroxy-[3H]hexadecanoic acid (HHA). High-molecularweight cutin became ester-bonded to intact [3H]HHA molecules, which thereby became unextractable except by ester-hydrolysing alkalis. In-situ CCT activity correlated with growth rate in Hylotelephium leaves and tomato fruits, suggesting a role in loosening the outer epidermal wall during organ growth. The only well-defined cutin transacylase in the apoplast, CUS1 (a tomato cutin synthase), when produced in transgenic tobacco, lacked CCT activity. This finding provides a reference for future CCT protein identification, which can adopt our sensitive enzyme assay to screen other CUS1-related enzymes.
U2 - 10.1042/BCJ20200835
DO - 10.1042/BCJ20200835
M3 - Journal article
C2 - 33511979
AN - SCOPUS:85101759910
VL - 478
SP - 777
EP - 798
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 4
ER -
ID: 306676215