Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes

Shuyu Zhang, W. G. Haldenwang

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Obg is a GTP-binding protein of Bacillus subtilis with essential, but undefined roles in the bacterium's growth, sporulation, and stress responses. Obg orthologs are widely conserved among both bacteria and eukaryotes. Gel filtration and affinity blot assays have suggested that Obg may be ribosome-associated. In the current work, we continue an examination of the putative Obg:ribosome interaction. Velocity centrifugation analyses of crude B. subtilis extracts or purified Obg:ribosome mixtures suggest that Obg is initially ribosome-bound, but can separate from ribosomes during sedimentation in the absence of added nucleotides. Addition of either GTP, GDP or ATP to the gradient prolonged the Obg:ribosome association, while inclusion of a nonhydrolyzable GTP analog (5-guanylyl-imidodiphosphate) preserved it. The data strengthen the notion that Obg is a ribosome-associated protein, demonstrate that Obg's association with ribosomes is stabilized by GTP, and indicate that the ribosome-bound Obg can likely hydrolyze GTP and be released as a consequence.

Original languageEnglish (US)
Pages (from-to)565-569
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Sep 17 2004


  • Bacillus subtilis
  • GTP
  • Obg
  • Ribosome

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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