Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145 |
| |
Authors: | András?Penyige author-information" > author-information__contact u-icon-before" > mailto:penyige@dote.hu" title=" penyige@dote.hu" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author,Judit?Keser?,Ferenc?Fazakas,Iván?Schmelczer,Krisztina?Szirák,Gy?rgy?Barabás,Sándor?Biró |
| |
Affiliation: | 1.Department of Human Genetics,University of Debrecen,Debrecen,Hungary;2.Clinical Research Center, Medical and Health Science Center,University of Debrecen,Debrecen,Hungary |
| |
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 SC05477 encode members of the family of periplasmic extracellular solute-binding proteins, and SCO6108 and SC01968 are secreted hydrolases. Dehydrogenases are encoded by SC04824 and SC04771. The other targets are GlnA (glutamine synthetase I., SC02198) and SpaA (starvation-sensing protein encoded by SC07629). 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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|