| Literature DB >> 8730873 |
J Oberto1, E Bonnefoy, E Mouray, O Pellegrini, P M Wikström, J Rouvière-Yaniv.
Abstract
The histone-like protein HU isolated from Escherichia coli exhibited, after several purification steps, a Mg(2+)-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 Mg(2+)-Mn(2+)-dependent endonuclease activity. This is an unexpected property for a ribosomal protein.Entities:
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Year: 1996 PMID： 8730873 DOI： 10.1111/j.1365-2958.1996.tb02476.x
Source DB: PubMed Journal: Mol Microbiol ISSN： 0950-382X Impact factor: 3.501