Literature DB >> 20433953

Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain.

Domenico De Rasmo1, 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.   

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, (32)P labelling and immunodetection show that "in vitro" PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. (32)P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein. (c) 2010 Mitochondria Research Society. Published by Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20433953     DOI: 10.1016/j.mito.2010.04.005

Source DB:  PubMed          Journal:  Mitochondrion        ISSN: 1567-7249            Impact factor:   4.160


  17 in total

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