PMID:11796219

Citation	Symmons, MF, Williams, MG, Luisi, BF, Jones, GH and Carpousis, AJ (2002) Running rings around RNA: a superfamily of phosphate-dependent RNases. Trends Biochem. Sci. 27:11-8
Abstract	The exosome of Saccharomyces cerevisiae and the degradosome of Escherichia coli are multienzyme complexes involved in the degradation of mRNA. Both contain enzymes that are similar to the phosphate-dependent exoribonuclease RNase PH. These enzymes are phosphorylases that degrade RNA from the 3'-end. A recent X-ray crystallographic study of the polynucleotide phosphorylase (PNPase) from Streptomyces antibioticus reveals, for the first time, the atomic structure of a member of the RNase PH superfamily. Here, information from the structure of PNPase is used to address two related issues. First, the structure supports the idea that PNPase, which is a trimer of multidomain subunits, arose by duplication of a gene encoding an RNase PH-like enzyme. Second, the structure might explain how RNase PH-like enzymes associate into oligomeric rings that degrade RNA in a processive reaction.
Links	PubMed
Keywords	Amino Acid Sequence; Escherichia coli/enzymology; Exoribonucleases/chemistry; Exoribonucleases/metabolism; Humans; Molecular Sequence Data; Polyribonucleotide Nucleotidyltransferase/chemistry; Protein Conformation; Protein Folding; RNA/chemistry; Saccharomyces cerevisiae/enzymology; Sequence Homology, Amino Acid
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