These authors contributed equally to this work.
The Escherichia coli ribosomal protein S16 is an endonuclease
Article first published online: 6 OCT 2006
Volume 19, Issue 6, pages 1319–1330, March 1996
How to Cite
Oberto, J., Bonnefoy, E., Mouray, E., Pellegrini, O., Wikström, P. M. and Rouvière-Yaniv, J. (1996), The Escherichia coli ribosomal protein S16 is an endonuclease. Molecular Microbiology, 19: 1319–1330. doi: 10.1111/j.1365-2958.1996.tb02476.x
- Issue published online: 6 OCT 2006
- Article first published online: 6 OCT 2006
- Received 23 October, 1995; revised 21 November, 1995; accepted 28 November, 1995
The histone-like protein HU isolated from Escherichia coli exhibited, after several purification steps, a Mg2+-dependent nuclease activity. We show here that this activity can be dissociated from HU by a denaturation-renaturation step, and is due to a small fraction of ribosomal protein S16 co-purifying with HU. S16 is an essential component of the 30S ribosomal particles. We have cloned, overproduced, and purified a histidine-tagged S16 and shown that this protein is a DNA-binding protein carrying a Mg2+-Mn2+-dependent endonuclease activity. This is an unexpected property for a ribosomal protein.