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legumin/arabidopsis thaliana
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Disulfide interchange reactions in 11S globulin subunits of Cruciferae seeds. Relationships to gene families.
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Cruciferin, the main storage protein in rapeseed (Brassica napus L.), is a legumin-like 11S globulin. Using SDS/PAGE cruciferin was shown to be composed of different subunits consisting of alpha S and beta S polypeptides, which were disulfide linked, and also closely related free alpha f and beta f
A T9G mutation in the prototype TATA-box TCACTATATATAG determines nucleosome formation and synergy with upstream activator sequences in plant promoters.
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We had earlier reported that mutations to G and C at the seventh and eighth positions in the prototype TATA-box TCACTATATATAG inhibited light-dependent activation of transcription from the promoter. In this study, we characterized mutations at the ninth position of the prototype TATA-box.
Patterns of protein oxidation in Arabidopsis seeds and during germination.
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Increased cellular levels of reactive oxygen species are known to occur during seed development and germination, but the consequences in terms of protein degradation are poorly characterized. In this work, protein carbonylation, which is an irreversible oxidation process leading to a loss of
A stress-associated protein containing A20/AN1 zing-finger domains expressed in Medicago truncatula seeds.
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MtSAP1 (Medicago truncatula stress-associated protein 1) was revealed as a down-regulated gene by suppressive subtractive hybridization between two mRNA populations of embryo axes harvested before and after radicle emergence. MtSAP1 is the first gene encoding a SAP with A20 and AN1 zinc-finger
The Amborella vacuolar processing enzyme family.
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Most vacuolar proteins are synthesized on rough endoplasmic reticulum as proprotein precursors and then transported to the vacuoles, where they are converted into their respective mature forms by vacuolar processing enzymes (VPEs). In the case of the seed storage proteins, this process is of major
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