Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 355425
Title Isolation and characterization of a tomato non-specific lipid transfer protein involved in polygalacturonase-mediated pectin degradation
Author(s) Tomassen, M.M.M.; Barrett, D.M.; Valk, H.C.P.M. van der; Woltering, E.J.
Source Journal of Experimental Botany 58 (2007)5. - ISSN 0022-0957 - p. 1151 - 1160.
Department(s) AFSG Quality in Chains
AFSG Biobased Products
Horticultural Supply Chains
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) beta-subunit - gene-expression - transgenic tomatoes - fruit - isoenzymes - plant - converter - ultrastructure - manipulation - conversion
Abstract An important aspect of the ripening process of tomato fruit is softening. Softening is accompanied by hydrolysis of the pectin in the cell wall by pectinases, causing loss of cell adhesion in the middle lamella. One of the most significant pectin-degrading enzymes is polygalacturonase (PG). Previous reports have shown that PG in tomato may exist in different forms (PG1, PG2a, PG2b, and PGx) commonly referred to as PG isoenzymes. The gene product PG2 is differentially glycosylated and is thought to associate with other proteins to form PG1 and PGx. This association is thought to modulate its pectin-degrading activity in planta. An 8 kDa protein that is part of the tomato PG1 multiprotein complex has been isolated, purified, and functionally characterized. This protein, designated `activator¿ (ACT), belongs to the class of non-specific lipid transfer proteins (nsLTPs). ACT is capable of `converting¿ the gene product PG2 into a more active and heat-stable form, which increases PG-mediated pectin degradation in vitro and stimulates PG-mediated tissue breakdown in planta. This finding suggests a new, not previously identified, function for nsLTPs in the modification of hydrolytic enzyme activity. It is proposed that ACT plays a role in the modulation of PG activity during tomato fruit softening.
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