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

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.
AuthorsAndrás Penyige, Judit Keseru, Ferenc Fazakas, Iván Schmelczer, Krisztina Szirák, György Barabás, Sándor Biró
JournalJournal of microbiology (Seoul, Korea) (J Microbiol) Vol. 47 Issue 5 Pg. 549-56 (Oct 2009) ISSN: 1976-3794 [Electronic] Korea (South)
PMID19851727 (Publication Type: Journal Article)
Chemical References
  • Bacterial Proteins
  • Adenosine Diphosphate Ribose
Topics
  • Adenosine Diphosphate Ribose (analysis)
  • Amino Acid Sequence
  • Bacterial Proteins (chemistry, isolation & purification)
  • Chromatography, Affinity
  • Electrophoresis, Gel, Two-Dimensional
  • Molecular Sequence Data
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Streptomyces coelicolor (chemistry)

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