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Nucleases: diversity of structure, function and mechanism

  • Wei Yang (a1)
Abstract
Abstract

Nucleases cleave the phosphodiester bonds of nucleic acids and may be endo or exo, DNase or RNase, topoisomerases, recombinases, ribozymes, or RNA splicing enzymes. In this review, I survey nuclease activities with known structures and catalytic machinery and classify them by reaction mechanism and metal-ion dependence and by their biological function ranging from DNA replication, recombination, repair, RNA maturation, processing, interference, to defense, nutrient regeneration or cell death. Several general principles emerge from this analysis. There is little correlation between catalytic mechanism and biological function. A single catalytic mechanism can be adapted in a variety of reactions and biological pathways. Conversely, a single biological process can often be accomplished by multiple tertiary and quaternary folds and by more than one catalytic mechanism. Two-metal-ion-dependent nucleases comprise the largest number of different tertiary folds and mediate the most diverse set of biological functions. Metal-ion-dependent cleavage is exclusively associated with exonucleases producing mononucleotides and endonucleases that cleave double- or single-stranded substrates in helical and base-stacked conformations. All metal-ion-independent RNases generate 2′,3′-cyclic phosphate products, and all metal-ion-independent DNases form phospho-protein intermediates. I also find several previously unnoted relationships between different nucleases and shared catalytic configurations.

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*Author for correspondence: W. Yang, Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 9000 Rockville Pike, Bldg. 5, Rm B1-03, Bethesda, MD 20892, USA. Email: wei.yang@nih.gov
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This list contains references from the content that can be linked to their source. For a full set of references and notes please see the PDF or HTML where available.

N. C. Horton (2008). DNA Nucleases. In Protein–Nucleic Acid Interactions (eds. P. A. Rice & C. C. Correll ), pp. 333363. Cambridge: Royal Society of Chemistry Publishing.

J. P. Muyrers , Y. Zhang & A. F. Stewart (2000). ET-cloning: think recombination first. Genetic Engineering (New York) 22, 7798.

W. Saenger (1984). Principles of Nucleic Acid Structure, New York, NY: Springer.

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Quarterly Reviews of Biophysics
  • ISSN: 0033-5835
  • EISSN: 1469-8994
  • URL: /core/journals/quarterly-reviews-of-biophysics
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