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FEBS Letters 372 (1995)238-242 FEBS 16062 Histidine and tyrosine phosphorylation in pea mitochondria
 

Summary: FEBS Letters 372 (1995)238-242 FEBS 16062
Histidine and tyrosine phosphorylation in pea mitochondria:
evidence for protein phosphorylation in respiratory redox signalling
Gunilla H~kansson*, John F. Allen
Plant Cell Biology, Lund Universit); Box 7007, S-220 07 Lund, Sweden
Received 11 August 1995
Abstract A 37 kDa protein in pea mitochondria was found to
contain phosphorylated residues. Phosphorylation was acid-labile
but stable in alkali solution, a unique property of phosphorylation
on histidine, indicating that a signal transduction pathway with
homology to bacterial two-component systems might exist in
plant mitochondria. We also describe the first example of tyrosine
phosphorylation in plant organelles and the first indication of
protein phosphorylation as part of a redox signalling mechanism
in mitochondria. Labelling of three proteins (28, 27 and 12 kDa)
was found to be dependent on the redox state of the reaction
medium. Their phospho-groups were resistant to alkali as well as
acid treatment and labelling was inhibited by the tyrosine kinase
inhibitor genistein.
Key words. Redox signalling; Tyrosine phosphorylation;

  

Source: Allen, John F. - School of Biological and Chemical Sciences, Queen Mary, University of London

 

Collections: Renewable Energy; Biology and Medicine