Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity.

@article{MotojimaMiyazaki2010RibosomalPL,
  title={Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity.},
  author={Yuko Motojima-Miyazaki and Masasuke Yoshida and Fumihiro Motojima},
  journal={Biochemical and biophysical research communications},
  year={2010},
  volume={400 2},
  pages={241-5}
}
Although eukaryotic Hsp90 has been studied extensively, the function of its bacterial homologue HtpG remains elusive. Here we report that 50S ribosomal protein L2 was found as an associated protein with His-tagged HtpG from Escherichia coli cultured in minimum medium at 45 °C. L2 specifically activated ATPase activity of HtpG, but other denatured proteins did not. The analysis using domain derivatives of HtpG and L2 showed that C-terminal domain of L2 and the middle to C-terminal domain of HtpG… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 22 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 49 references

HtpG

  • T. Sato, S. Minagawa, E. Kojima, N. Okamoto, H. Nakamoto
  • the prokaryotic homologue of Hsp90, stabilizes a…
  • 2010
3 Excerpts

Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals

  • R. S. Gupta
  • plants, and fungi species, Mol. Biol. Evol. 12…
  • 2010
1 Excerpt

Similar Papers

Loading similar papers…