Specific reduction of wheat storage proteins by thioredoxin h.

Abstract:

:Gliadins and glutenins, the major storage proteins of wheat endosperm (Triticum durum, Desf. cv Monroe), were reduced in vitro by the NADP/thioredoxin system (NADPH, NADP-thioredoxin reductase and thioredoxin; in plants, the h type) from either the same source or the bacterium Escherichia coli. A more limited reduction of certain members of these protein groups was achieved with the reduced form of glutathione or glutaredoxin, a protein known to replace thioredoxin in certain bacterial and mammalian enzyme systems but not known to occur in higher plants. Endosperm extracts contained the enzymes necessary to reduce NADP by the oxidative pentose phosphate pathway (hexokinase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase). The gliadins and glutenins were also reduced in vivo during germination--an event that accompanied their proteolytic breakdown. The results suggest that thioredoxin, reduced by NADPH generated via the oxidative pentose phosphate pathway, functions as a signal in germination to enhance metabolic processes such as the mobilization of storage proteins and, as found earlier, the activation of enzymes.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Kobrehel K,Wong JH,Balogh A,Kiss F,Yee BC,Buchanan BB

doi

10.1104/pp.99.3.919

subject

Has Abstract

pub_date

1992-07-01 00:00:00

pages

919-24

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

99

pub_type

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