PMID:8730873

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Citation

Oberto, J, Bonnefoy, E, Mouray, E, Pellegrini, O, Wikström, PM and Rouvière-Yaniv, J (1996) The Escherichia coli ribosomal protein S16 is an endonuclease. Mol. Microbiol. 19:1319-30

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.

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Keywords

Bacterial Proteins/isolation & purification; Base Sequence; DNA Primers/genetics; DNA, Bacterial/genetics; DNA-Binding Proteins/isolation & purification; Endonucleases/genetics; Endonucleases/isolation & purification; Endonucleases/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Magnesium/metabolism; Manganese/metabolism; Molecular Sequence Data; Ribosomal Proteins/genetics; Ribosomal Proteins/isolation & purification; Ribosomal Proteins/metabolism

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