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Post-translational modification of enzymes in non photosynthetic plastids of higher plants

ReferenceC01261
Principal Investigator / Supervisor Professor Michael Emes
Co-Investigators /
Co-Supervisors
Institution The University of Manchester
DepartmentLife Sciences
Funding typeResearch
Value (£) 149,629
StatusCompleted
TypeResearch Grant
Start date 01/02/1994
End date 01/07/1997
Duration41 months

Abstract

Root plastids are a focal site of nitrogen assimilation and amino acid synthesis in plants. We have found that 3 soluble proteins of molecular size 62, 58 and 41 kDa can be phosphorylated in pea root plastids. Phosphorylation of the 62 kDa protein is abolished in the presence of glucose-6-phosphate, whilst phosphorylation of the 58 kDa protein is abolished in the presence of 2-oxoglutarate. The aim of this project is to determine the identity of the proteins being phosphorylated by protein sequency and oligonucleotide probing of a cDNA library; to characterise the effects of phosphorylation on their biological activities; and to purify and characterise the protein kinases involved.

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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