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Histidine and tyrosine phosphorylation in pea mitochondria: evidence for protein phosphorylation in respiratory redox signalling
Author(s) -
Håkansson Gunilla,
Allen John F.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00990-q
Subject(s) - phosphorylation , tyrosine phosphorylation , protein phosphorylation , biochemistry , phosphorylation cascade , tyrosine , mitochondrion , oxidative phosphorylation , protein tyrosine phosphatase , histidine , biology , microbiology and biotechnology , chemistry , protein kinase a , amino acid
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.