Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2068897 | Mitochondrion | 2010 | 8 Pages |
Abstract
The NDUFS4 subunit of complex I of the mammalian respiratory chain has a fully conserved carboxy-terminus with a canonical RVSTK phosphorylation site. Immunochemical analysis with specific antibodies shows that the serine in this site of the protein is natively present in complex I in both the phosphorylated and non-phosphorylated state. Two-dimensional IEF/SDS–PAGE electrophoresis, 32P labelling and immunodetection show that “in vitro” PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. 32P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biophysics
Authors
Domenico De Rasmo, Giuseppe Palmisano, Salvatore Scacco, Zuzana Technikova-Dobrova, Damiano Panelli, Tiziana Cocco, Anna Maria Sardanelli, Antonio Gnoni, Loris Micelli, Antonio Trani, Aldo Di Luccia, Sergio Papa,