Award details

Plant and fungal ornithine decarboxylases and antizymes

Reference	BBS/E/F/04330948
Principal Investigator / Supervisor	Dr Anthony Michael
Co-Investigators / Co-Supervisors
Institution	Quadram Institute Bioscience
Department	Quadram Institute Bioscience Department
Funding type	Research
Value (£)	57,372
Status	Completed
Type	Institute Project
Start date	01/04/1997
End date	30/09/1999
Duration	30 months

Abstract

Ornithine decarboxylase (ODC) is the first and key step in polyamine biosynthesis in animals, yeast and fungi. In plants, an additional pathway for polyamine production is present due to the enzyme arginine decarboxylase. In vertebrates, ODC is a very short-lived protein and is highly regulated. High levels of polyamines repress ODC activity by activating an ODC antizyme, which binds to the ODC protein allowing degradation of ODC by the 26S proteosome. The antizyme messenger RNA is present in all cells but due to the presence of a stop codon, the antizyme protein cannot be produced. However, high levels of polyamines cause frame- shifting of the antizyme mRNA leading to read-through of the stop codon, thereby producing the functional antizyme protein. It is thought that the yeast ODC is also regulated at the post translational level but not by an antizyme. The plant ODC, apparently, may be regulated by an antizyme. We will use the yeast two-hybrid system, that allows the in vivo detection of protein protein interactions, to clone proteins that bind to the yeast and Arabidopsis ODC.

Summary

unavailable

Committee	Closed Committee - Plant & Microbial Sciences (PMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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