PMID:9502433

Citation	Zhang, P, Vigne, JL and Mellon, SH (1998) Polyribonucleotide phosphorylase is a double-stranded DNA-binding protein. DNA Cell Biol. 17:169-75
Abstract	Polyribonucleotide phosphorylase (PNPase) is one of the critical components of the E. coli RNA degradosome, which consists of both PNPase and endoribonuclease RNase E. The function of this complex is to control the rate of mRNA degradation. The PNPase possesses two enzymatic activities, namely 3'-5' processive exoribonuclease activity and 5'-3' RNA polymerase activity. In the present study, we used conventional chromatography to purify an E. coli protein that binds to a specific double-stranded DNA sequence. Microsequencing of the purified protein showed that this DNA-binding protein was PNPase. Our data further demonstrate that PNPase binds to DNA in a sequence-specific manner. These data suggest that PNPase may have previously unappreciated DNA-related functions in addition to its known role in mRNA degradation.
Links	PubMed
Keywords	Amino Acid Sequence; Chromatography, Ion Exchange; DNA, Bacterial/metabolism; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; Polyribonucleotide Nucleotidyltransferase/isolation & purification; Polyribonucleotide Nucleotidyltransferase/metabolism; Protein Binding
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