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Specificity of the S1 nuclease from Aspergillus oryzae


, : Specificity of the S1 nuclease from Aspergillus oryzae. Journal of Biological Chemistry 250(22): 8848-8855

Conditions are described for digesting single-stranded DNA by S1 nuclease without introducing breaks in double-stranded DNA. The enzyme is inhibited by low concentrations of various compounds of phosphate. Under certain conditions S1 nuclease cleaves the strand opposite a nick in bacteriophage T5 DNA; under other conditions, the enzyme cleaves a loop in one strand of heteroduplex lambdaDNA while leaving the opposite strand intact. S1 nuclease makes many single strand breaks in ultraviolet-irradiated duplex lambdaDNA. Superhelical DNA of phiX174 (Form I) is converted first to a relaxed circular molecule (Form II), and then to a linear molecule (Form III) by cleavage at one site per molecule. Since the cleavage occurs at many sites in the population of molecules, the partially single-stranded regions in phiX174 superhelical DNA are not determined by specific nucleotide sequences.

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Accession: 041408264

PMID: 171268

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Related references

Wiegand, R.C.; Godson, G.N.; Radding, C.M., 1975: Specificity of the s 1 nuclease from aspergillus oryzae. Journal of Biological Chemistry 250(22): 8848-8555

Karpeiskii M.Ya; Senchenko V.N.; Yakovlev G.I.; Kolbanovskaya E.Yu, 1982: Substrate specificity of nuclease s 1 from aspergillus oryzae in hydrolysis of low molecular weight substrates. The hydrolysis of low molecular weight substrates by nuclease S1 from A. oryzae was studied. The enzyme showed no specificity either towards the nature of heterocyclic base or that of ribose moiety on the stage of the enzyme-substrate complex form...

Kolbanovskaya E.Yu, 1982: A study of the substrate specificity of nuclease s 1 from aspergillus oryzae in the hydrolysis of low molecular weight substrates. Soviet Journal Of Bioorganic Chemistry: 204

Hino, T.U.zumi, T.T.mura, G.A.ima, K., 1971: Studies on the autolysis of Aspergillus oryzae. X. Mode of action and base specificity of crystalline nuclease O. Agricultural and biological chemistry: 35 (7) 1109-1115

Karpeiskii, M.; Senchenko, V.1; Yakovlev, G.1; Kobanovskaya, E., 1983: A study of the substrate specificity of nuclease S1 from Aspergillus oryzae in the hydrolysis of low-molecular-weight substrates Fungi. Soviet journal of bioorganic chemistry(pub 1983) 8(3): 196-204

Hino T.; Uozumi T.; Tamura G.; Arima K., 1971: Studies on the autolysis of aspergillus oryzae part 10 mode of action and base specificity of crystalline nuclease o. Agricultural & Biological Chemistry 35(7): 1109-1115

Reddy, L.G.; Shankar, V., 1987: Immobilization of single-strand specific nuclease (S1 nuclease) from Aspergillus oryzae. S1 nuclease from Aspergillus oryzae (EC 3.1.30.1) was coupled to gelatin-alginate composite matrix using the residual free aldehyde groups on the surface of glutaraldehyde crosslinked matrix. The immobilized enzyme retained approximately 10% activ...

Uozumi, T.; Ishino, K.; Beppu, T.; Arima, K., 1976: Purification and properties of the nuclease inhibitor of Aspergillus oryzae and kinetics of its interaction with crystalline nuclease O. A nuclease inhibitor found in the mycelia of Aspergillus oryzae has been purified 158,000-fold by ammonium sulfate precipitation, chromatography on Sephadex G-75, DEAE-Sephadex A-50 and Bio-Gel p-60 columns, preparative disc electrophoresis on acr...

Uozumi, T.; Ishino, K.; Beppu, T.; Arima, K., 1976: Purification and properties of the nuclease inhibitor of aspergillus oryzae and kinetics of its interaction with crystalline nuclease o ec 3.1.4.9. A nuclease inhibitor found in the mycelia of A. oryzae was purified 158,000-fold by ammonium sulfate precipitation, chromatography on Sephadex G-75, DEAE-Sephadex A-50 and Bio-Gel P-60 columns, preparative disc electrophoresis on acrylamide gel, a...

Rushizky, G.W., 1981: S1 nuclease of Aspergillus oryzae. S1 nuclease has found many uses in the analysis of the structure of nucleic acids, and more new applications, such as the mapping of splice points of early mRNAs in SV40, will undoubtedly be found.