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PLANT PHYSIOLOGY , Vol 114, Issue 4 1547-1556, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Characterization and Functional Expression of a Ubiquitously Expressed Tomato Pectin Methylesterase
J. Gaffe, M. E. Tiznado and A. K. Handa
Department of Horticulture, Purdue University, 1165 Horticulture Building, West Lafayette, Indiana 47907-1165
Pectin methylesterase (PME),a ubiquitous enzyme in plants, de-esterifies
the methoxylated pectin in the plant cell wall. We have characterized a PME
gene (designated as pmeu1) from tomato (Lycopersicon esculentum) with an
expression that is higher in younger root, leaf, and fruit tissues than in
older tissues. Hypocotyls and epicotyls show higher accumulation of pmeu1
transcripts compared with cotyledons. pmeu1 represents a single-copy gene
in the tomato genome. Comparison of the deduced amino acid sequence of
pmeu1 with other PME homologs showed that the N-terminal halves are highly
variable, and the C-terminal halves are relatively conserved in plant PMEs.
Constitutive expression of a fruit-specific PME antisense gene does not
affect the level of pmeu1 transcripts in vegetative tissues but does lower
the level of PMEU1 mRNA in developing tomato fruits. These results suggest
that there exists developmentally regulated silencing of pmeu1 by a
heterologous PME antisense gene. Expression of pmeu1 in tobacco (Nicotiana
tabacum) under the control of the cauliflower mosaic virus 35S promoter
caused up to a 4-fold increase in PME specific activity that was correlated
with the accumulation of PMEU1 mRNA. In vitro transcription-translation
analyses show that pmeu1 encodes a 64-kD polypeptide, whereas transgenic
tobacco plants expressing pmeu1 accumulate a new 37-kD polypeptide,
suggesting extensive posttranslational processing of PMEU1. These results
are the first evidence, to our knowledge, of the functional
characterization of a PME gene and the extensive modification of the
encoded polypeptide.
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