A thermostable, sequence-specific restriction endonuclease from Bacillus stearothermophilus: BstPI.
AUTOR(ES)
Pugatsch, T
RESUMO
A restriction endonuclease, BstPI, was purified from a strain of B. stearothermophilus, and its cleavage specificity was determined. The enzyme cleaves at palindromic sites of the general structure: (Formula: see text) where N.N' can be any base pair. It produces phosphorylated 5'-termini which are single stranded over a length of 5 nucleotides. Ends generated by cleavage with BstPI can be rejoined by DNA ligase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=342318Documentos Relacionados
- A thermostable sequence-specific endonuclease from Thermus aquaticus.
- Thermostable, Raw-Starch-Digesting Amylase from Bacillus stearothermophilus
- A sequence-specific endonuclease (Xmn I) from Xanthomonas manihotis.
- BstBSI, a restriction endonuclease from Bacillus stearothermophilus BS which recognizes 5'GTATAC3'.
- ScrFI: a new sequence-specific endonuclease from Streptococcus cremoris.
