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Mitochondrial cytochrome c oxidase subunit IV is phosphorylated by an endogenous kinase
Author(s) -
Steenaart Nancy A.E.,
Shore Gordon C.
Publication year - 1997
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/s0014-5793(97)01145-9
Subject(s) - phosphoprotein , cytochrome c oxidase , protein subunit , phosphorylation , biochemistry , inner mitochondrial membrane , protein kinase a , protein phosphorylation , microbiology and biotechnology , mitochondrion , cytochrome c , polyacrylamide gel electrophoresis , chemistry , biology , enzyme , gene
This study was undertaken to identify novel mitochondrial membrane proteins that are potential targets for phosphorylation. Mitochondrial membranes were incubated in the presence of [γ‐ 32 P]ATP and the Triton X‐114 extractable protein was subjected to ion‐exchange and polyacrylamide gel chromatography to purify a major phosphorylated protein of approximately 17 000 Da. The determined peptide sequence of the purified phosphoprotein corresponded to a segment of cytochrome c oxidase subunit IV, an inner membrane protein of 17 160 Da. The identity of the phosphoprotein was confirmed by two‐dimensional electrophoresis and Western blotting. The results identify mitochondrial cytochrome c oxidase subunit IV as a protein which is phosphorylated by an endogenous kinase.