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- Disruption of SCO5461 Gene Coding for a Mono-ADP-Ribosyltransferase Enzyme Produces a Conditional Pleiotropic Phenotype Affecting Morphological Differentiation and Antibiotic Production in Streptomyces coelicolor
- Krisztina Szirák , Judit Keser&# , Sándor Biró , Iván Schmelczer , György Barabás , András Penyige
- J. Microbiol. 2012;50(3):409-418. Published online June 30, 2012
- DOI: https://doi.org/10.1007/s12275-012-1440-y
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- 9 Scopus
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Abstract
- The SCO5461 gene of Streptomyces coelicolor A3(2) codes for an ADP-ribosyltransferase enzyme that is predicted to be a transmembrane protein with an extracellular catalytic domain. PCR-targeted disruption of the gene resulted in a mutant that differentiated normally on complex SFM medium; however, morphological differentiation in minimal medium was significantly delayed and this phenotype was even more pronounced on osmotically enhanced minimal medium. The mutant did not sporulate when it was grown on R5 medium, however the normal morphological differentiation was restored when the strain was cultivated beside the wild-type S. coelicolor M145 strain. Comparison of the pattern of ADP-ribosylated proteins showed a difference between the mutant and the wild type, fewer modified proteins were present in the cellular crude extract of the mutant strain. These results support our previous suggestions that protein ADP-ribosylation is involved in the regulation of differentiation and antibiotic production and secretion in Streptomyces.
- 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
- 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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- 11 Scopus
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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.
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