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Characterization of the Specific DNA Nicking Activity of Restriction Endonuclease N.BstNBI
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R.D. Morgan
Published/Copyright:
July 5, 2005
Abstract
N.BstNBI is a unique restriction endonuclease isolated from Bacillus stearothermophilus. We have characterized the recognition sequence and the cleavage site of N.BstNBI. Mapping of cleavage sites of N.BstNBI showed that it recognizes an asymmetric sequence, 5′ GAGTC 3′, and cleaves only on the top strand 4 base pairs away from its recognition sequence. To verify the nicking activity of N.BstNBI, we have constructed two plasmids containing a single recognition sequence (pNB1) or no recognition site (pNB0). When pNB1 and pNB0 were incubated with the enzyme, N.BstNBI nicked only the plasmid pNB1, suggesting that N.BstNBI is a specific nicking endonuclease.
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Published Online: 2005-07-05
Published in Print: 2000-11-15
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Purification and Cloning of Type A/B hnRNP Proteins Involved in Transcriptional Activation from the Rat spi 2 Gene GAGA Box
- Release of Ribosome-Bound 5S rRNA upon Cleavage of the Phosphodiester Bond between Nucleotides A54 and A55 in 5S rRNA
- Noncovalent Binding of Poly(ADP-Ribose) to Nuclear Matrix Proteins: Developmental Changes and Tissue Specificity
- Mutational Analysis of Two PWW Sequence Motifs in Human Aminoacylase 1
- Divergent Enzyme Kinetics and Structural Properties of the Two Human Mitochondrial Creatine Kinase Isoenzymes
- Cloning, Heterologous Expression and Kinetic Analysis of Glycerol Kinase (TbGLK1) from Trypanosoma brucei
- Identification of the 50S Ribosomal Proteins from the Eubacterium Thermus thermophilus
- The Hyper-Thermostable Fe-Superoxide Dismutase from the Archaeon Acidianus ambivalens: Characterization, Recombinant Expression, Crystallization and Effects of Metal Exchange
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- Kinetic and Thermodynamic Analysis of Leech-Derived Tryptase Inhibitor Interaction with Bovine Tryptase and Bovine Trypsin
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