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Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145

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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 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.

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Authors and Affiliations

  1. Department of Human Genetics, University of Debrecen, Debrecen, Nagyerdei krt 98, H-4032, Hungary

    András Penyige, Judit Keserű, Iván Schmelczer, Krisztina Szirák, György Barabás & Sándor Biró

  2. Clinical Research Center, Medical and Health Science Center, University of Debrecen, Debrecen, Nagyerdei krt 98, H-4032, Hungary

    Ferenc Fazakas

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  1. András Penyige
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  2. Judit Keserű
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  3. Ferenc Fazakas
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  4. Iván Schmelczer
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  5. Krisztina Szirák
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  6. György Barabás
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  7. Sándor Biró
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Correspondence to András Penyige.

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Penyige, A., Keserű, J., Fazakas, F. et al. Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145. J Microbiol. 47, 549–556 (2009). https://doi.org/10.1007/s12275-009-0032-y

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