BstF5I, a new restriction endonuclease (ENase) from Bacillus stearothermophilus F5, has been discovered. This enzyme recognizes 5'-GGATG-3' and cleaves DNA, generating a 2-base 3'extension: 5'-GGATG NN[symbol: see text]-3' 3'-CCTAC[symbol: see text]NN-5' BstF5I is an isoschizomer of FokI and seems to be evolutionarily close to other nonpalindromic-recognizing ENases from thermophilic bacilli.
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http://dx.doi.org/10.1016/0378-1119(96)85083-9 | DOI Listing |
PLoS One
February 2016
Science for Life Laboratory, KTH, Gene Technology, Solna, 171 65, Sweden.
Restriction enzymes that recognize specific sequences but cleave unknown sequence outside the recognition site are extensively utilized tools in molecular biology. Despite this, systematic functional categorization of cleavage performance has largely been lacking. We established a simple and automatable model system to assay cleavage distance variation (termed slippage) and the sequence dependence thereof.
View Article and Find Full Text PDFAnaerobe
October 2005
Institute of Animal Physiology and Genetics, Czech Academy of Sciences, Videnska 1083, 14220 Prague 4, Czech Republic.
Thirty-five strains of ruminal bacteria belonging to the former Butyrivibrio fibrisolvens species were screened for the presence of site-specific restriction endonuclease and modification methyltransferase activities. Seven strains possessed endonuclease activities detectable in crude cell extracts. The recognition sequences and optimal reaction conditions for seven of them were determined.
View Article and Find Full Text PDFGene
March 1997
SibEnzyme, Novosibirsk, Russia.
The gene for BstF5I-1 DNA-methyltransferase (MTase) from Bacillus stearothermophilus F5 (a FokI isoschizomer, recognizing 5'-GGATG-3') was cloned and its nucleotide (nt) sequence was determined. Analysis of deduced amino acid (aa) sequence shows that M x BstF5I-1 belongs to D21 class of MTases and has a little homology with M x FokI. M x BstF5I-1 modifies only the upper strand of recognition sequence (5'-GGATG-3').
View Article and Find Full Text PDFBstF5I, a new restriction endonuclease (ENase) from Bacillus stearothermophilus F5, has been discovered. This enzyme recognizes 5'-GGATG-3' and cleaves DNA, generating a 2-base 3'extension: 5'-GGATG NN[symbol: see text]-3' 3'-CCTAC[symbol: see text]NN-5' BstF5I is an isoschizomer of FokI and seems to be evolutionarily close to other nonpalindromic-recognizing ENases from thermophilic bacilli.
View Article and Find Full Text PDFNucleic Acids Res
February 1992
Department of Biotechnology, Tottori University, Japan.
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