Analysis and Identification of ADP-Ribosylated Proteins of Streptomyces coelicolor M145

András Penyige; Judit Keser&#; Ferenc Fazakas; Iván Schmelczer; Krisztina Szirák; György Barabás; Sándor Biró

doi:10.1007/s12275-009-0032-y

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Analysis and Identification of ADP-Ribosylated Proteins of Streptomyces coelicolor M145: András Penyige ¹, Judit Keser&# ^369;1, Ferenc Fazakas ², Iván Schmelczer ¹, Krisztina Szirák ¹, György Barabás ¹, Sándor Biró ¹; Journal of Microbiology 2009;47(5):549-556.
DOI: https://doi.org/10.1007/s12275-009-0032-y
Published online: October 24, 2009

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

Corresponding author: András Penyige , Tel: 36-52-416-531,

Received: 2 February 2009 • Accepted: 26 May 2009

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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.

Keywords: protein ADP-ribosylation;S. coelicolor;2D-PAGE;MALDI-TOF

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Analysis and Identification of ADP-Ribosylated Proteins of Streptomyces coelicolor M145

J. Microbiol. 2009;47(5):549-556. Published online October 24, 2009

DOI: https://doi.org/10.1007/s12275-009-0032-y

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