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Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons.

I Hara-Nishimura1, M Nishimura

  • 1Research Institute for Biochemical Regulation, School of Agriculture, Nagoya University, Chikusa, Nagoya 464 Japan.

Plant Physiology
|October 1, 1987
PubMed
Summary
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Pumpkin cotyledon vacuoles contain a thiol protease that converts proglobulin to globulin. This enzyme, localized in the vacuole matrix, increases during seed development and shows similar activity in castor bean protein bodies.

Area of Science:

  • Plant Biochemistry
  • Protease Function
  • Seed Development

Background:

  • Proglobulin conversion to globulin is crucial for seed storage proteins.
  • Vacuoles play a key role in post-translational modification of proteins.

Purpose of the Study:

  • Investigate the enzymic conversion of proglobulin to globulin in pumpkin cotyledons.
  • Characterize the enzyme responsible for this processing and its localization.

Main Methods:

  • Subcellular fractionation of pumpkin cotyledon vacuoles.
  • In vitro assay using radiolabeled proglobulin as substrate.
  • Inhibition and activation studies with various reagents.
  • Suborganellar fractionation of vacuoles and protein bodies.

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Main Results:

  • Vacuolar extracts catalyzed proglobulin to globulin conversion, producing gamma and delta polypeptide chains.
  • The optimal pH for conversion was 5.0.
  • The enzyme was identified as a thiol protease, inhibited by thiol reagents and activated by dithiothreitol/cysteine.
  • Activity was localized in the vacuole matrix and increased during seed development.
  • Similar activity was found in castor bean protein body matrix.

Conclusions:

  • Pumpkin vacuoles contain a thiol protease in their matrix responsible for proglobulin processing.
  • This enzyme's activity is developmentally regulated and conserved across species.