Restriction endonuclease T.Smu451I with new cleavage specificity-neoschizomer of T.AsuI

. 2021 Aug ; 66 (4) : 651-657. [epub] 20210505

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid33950513
Odkazy

PubMed 33950513
DOI 10.1007/s12223-021-00874-0
PII: 10.1007/s12223-021-00874-0
Knihovny.cz E-zdroje

A specific type II restriction endonuclease T.Smu451I has been purified to electrophoretic homogeneity from the frozen cells of soil bacterium Sphingobacterium multivorum 451 (formerly Flavobacterium multivorum 451), using ultrasonic grinding, nucleic acid removal by streptomycin sulfate, protein precipitation by ammonium sulfate and phosphocellulose P-11, DEAE-Cellulose DE-52, Hepharin-Sepharose CL-6B chromatography, and elucidated several characteristics of T.Smu451I. The molecular weight of the enzyme determined by gel filtration and SDS-polyacrylamide gel electrophoresis was calculated to be 45,000 ± 2000 D (dimer) and 23,000 ± 1000 D (monomer), respectively. The isoelectric point (pI) of T.Smu451I is 5.4. T.Smu451I recognizes pentanucleotide palindromic sequences 5'-GGNC↓C-3' and cleaves between C and C in position shown by arrow to produce 3'-cohesive terminus of trinucleotide. Therefore, T.Smu451I is a neoschizomer of T.AsuI.

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Arnold DA, Handa N, Kobayashi I, Kowalczykowski SC (2000) A novel, 11-nucleotide variant of X, X*: one of a class of sequences defining the E. coli recombination hotspot. X J Mol Biol 300:469–479 DOI

Atack MJ, Yang Y, Seib LK, Zhou Y, Je PM (2018) A survey of Type III restriction-modification systems reveals numerous, novel epigenetic regulators controlling phase-variable regulons; phasevarions. Nucleic Acids Res 46:1–11 DOI

Belkebir A, Azeddoug H (2012) Purification and characterization of SepII a new restriction endonuclease from Staphylococcus epidermides. Microbiol Res 167:90–94 DOI

Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram utilizing the principle of protein−dye binding. Anal Biochem 72:248–254 DOI

Deibert M, Grazulis S, Sasnauskas G, Siksnys V, Huber R (2000) Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA. Nature Struct Biol 7:792–799 DOI

Fuchs C, Rosenvold CE, Honingman A, Szybalski W (1980) Identification of palindromic sequence recognized by restriction endonuclease as based on the tabularized sequence data for seven viral and plasmid DNAs. Gene 10:357–370 DOI

Geerlof A (2008) Cloning using restriction enzymes. European Molecular Biology Laboratory, Hamburg Retrieved, pp 6–70

Janulaitis G, Timulaitiene G, Jovaisaite V, Tamulaitis G, Songailiens I, Munakova E et al (2017) Restriction endonuclease AgeI is a monomer which dimerizes to cleavage DNA. Nucleic Acids Res 45:3547–3558

Jeltsch A, Kroger M, Pingoud A (1995) Evidence for an evolutionary relationship among type-II restriction endonucleases. Gene 160:7–16 DOI

Kaczorowski T, Skowron PT (1989) Purification and characterization of the FokI restriction endonuclease. Gene 80:209–216 DOI

Kong H, Lee-Fong L, Porter N, Stickei S, Robert JR (2000) Fanctional analysis of putative restriction-modification system genes in the Helicobacter pylori J99 genome. Nucleic Acids Res 28:3216–3223 DOI

Kostiuk G, Dikis J, Sechwaks FW et al (2017) The dynamics of the monomeric restriction endonuclease BcnI during its interaction with DNA. Nucleic Acids Res 45:5968–5979 DOI

Krieg NR, Staley JT et al (2010) Bergey’s manual of systematic bacteriology, 2nd edn.4. Springer, New York, 330−339

Laemmli UK (1970) Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 277:680–685 DOI

Massey A, Kreuzer H (2001) Recombinant DNA and biotechnology: A guide for students ASM Press Washington, D.C 1−55581−176−0

Modrich P, Zabel D (1976) EcoRI endonuclease. Physical and catalytic properties of the homogeneous enzyme. J Biol Chem 251:5866–5874 DOI

Orlowski J, Bujnicki JM (2008) Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses. Nucleic Acids Res 36:3552–3569 DOI

Ra S-R, Kim M-S, Paek C-I, Pak Y-C, Pak S-H, Pak H-B, Ri K-C (2019) Bci528I, a new isoschizomer of EcoRI isolated from Bacillus circulans 528. Folia Microbiol 64:803–808 DOI

Roberts JR, Belfort M, Bestor T, Bhagwat AS et al (2003) A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. Nucleic Acids Res 31:1805–1812 DOI

Roberts JR, Vincze T, Posfai J, Macelis D (2015) REBASE-a database for DNA restriction and modification enzymes, genes and genomes. Nucleic Acids Res 43:Database issue D298−D299

Sambrook J, Russell DW (2001) Molecular cloning: a laboratory manual, 3rd edn. Cold Spring Harbor Laboratory Press, New York, pp 5–200

Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74:5463–5499 DOI

Shen WB, Heiter FD, Lunnen DK, Wilson GG, Stoddard LB (2017) DNA recognition by the SwaI restriction endonuclease involves unusual distortion of an 8 basepair A:T-rich target. Nucleic Acids Res 45:1516–1528 DOI

Viadiu H, Aggarwal AK (2000) Structure of BamHI bound to nonspecific DNA: A model for DNA sliding. Mol Cell 5:589–595 DOI

Zaremba1 M, Toliusis P, Grigaitis R, Manakova E, Silanskas A, Tamulaitiene G, Szczelkun M D, Siksnys V (2014) DNA cleavage by CglI and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis. Nucleic Acids Res 42:13887–13896

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