| Title |
Analysis and Identification of ADP-Ribosylated Proteins of Streptomyces coelicolor M145 |
| Author |
András Penyige1*, Judit Keserű1, Ferenc Fazakas2, Iván Schmelczer1, Krisztina Szirák1, György Barabás1, and Sándor Biró1 |
| Address |
1Department of Human Genetics, University of Debrecen, Debrecen, Nagyerdei krt 98, H-4032, Hungary, 2Clinical Research Center, Medical and Health Science Center, University of Debrecen, Debrecen, Nagyerdei krt 98, H-4032, Hungary |
| Bibliography |
Journal of Microbiology, 47(5),549-556, 2009,
|
| DOI |
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| Key Words |
protein ADP-ribosylation, S. coelicolor, 2D-PAGE, MALDI-TOF |
| Abstract |
Mono-ADP-ribosylation is the enzymatic transfer of ADP-ribose from NAD+ to acceptor proteins catalyzed by ADP-ribosyltransferases. Using m-aminophenylboronate affinity chromatography, 2D-gel electrophoresis, in-gel digestion and MALDI-TOF analysis we have identified eight in vitro ADP-ribosylated proteins in Streptomyces coelicolor, which can be classified into three categories: (i) secreted proteins; (ii) metabolic enzymes using NAD+/NADH or NADP+/NADPH as coenzymes; and (iii) other proteins. The secreted proteins could be classified into two functional categories: SCO2008 and SCO5477 encode members of the family
of periplasmic extracellular solute-binding proteins, and SCO6108 and SCO1968 are secreted hydrolases. Dehydrogenases are encoded by SCO4824 and SCO4771. The other targets are GlnA (glutamine synthetaseI., SCO2198) and SpaA (starvation-sensing protein encoded by SCO7629). SCO2008 protein and GlnA had been identified as ADP-ribosylated proteins in previous studies. With these results we provided experimental support for a previous suggestion that ADP-ribosylation may regulate membrane transport and localization of periplasmic proteins. Since ADP-ribosylation results in inactivation of the target protein, ADP-ribosylation of dehydrogenases might modulate crucial primary metabolic pathways in Streptomyces. Several of the proteins identified here could provide a strong connection between protein ADP-ribosylation and the regulation of morphological differentiation in S. coelicolor. |
