Mechanism for the selective conjugation of ubiquitin to phytochrome
Technical Report
·
OSTI ID:6605340
The long term goal of this project is to understand at the molecular level how intracellular proteins are degraded. The purpose of this research is to characterize the form-dependent degradation of phytochrome as a model system for the study of selective protein breakdown. Phytochrome exists in two photo-interconveretible forms, a red-absorbing Pr form and a far-red absorbing Pfr form. Recent evidence indicates that selective breakdown of phytochrome in etiolated oat seedlings occurs by a ubiquitin-dependent proteolytic pathway. Ubiquitin is a 76 amino acid eukaryotic protein that is covalently ligated to proteins destined for catabolism and serves as recognition signal for proteases specific for ubiquitin-protein conjugates. In an attempt to understand why Pfr and not Pr is recognized by the ubiquitin pathway, we have characterized ubiquitin-phytochrome conjugates (Ub-P) with respect to their kinetics of accumulation, localization within the cell, and sites of ubiquitin attachment. We also examined Pfr degradation in etiolated seedlings from a variety of other plant species (corn, rye, pea and zucchini squash) for their ability to form Ub-P during Pfr degradation. 4 refs.
- Research Organization:
- Wisconsin Univ., Madison, WI (USA). Dept. of Horticulture
- Sponsoring Organization:
- DOE/ER
- DOE Contract Number:
- FG02-88ER13968
- OSTI ID:
- 6605340
- Report Number(s):
- DOE/ER/13968-T2; ON: DE90017561
- Country of Publication:
- United States
- Language:
- English
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