Biopolym. Cell. 1985; 1(5):234-241.
http://dx.doi.org/10.7124/bc.000188
Reviews
Synthesis on single-stranded circular phage M13 DNA by DNA polymerase of nuclear silkworm polyhedrosis virus
1Ataeva D. O., 1Marlyev K. A., 1Kullyev P. K., 2Mikhailov V. S.
  1. Institute of Zoology, Academy of Sciences of the Turkmen SSR
    Ashkhabad, USSR
  2. N. K. Koltsov Institute of Developmental Biology, Academy of Sciences of the USSR
    Moscow, USSR

Abstract

A virus-induced DNA polymerase (B. m. NPV polymerase) was purified from the silkworm Bombyx mori pupae infected with nuclear polyhedrosis virus (B. m. NPV). NPV polymerase is a polypeptide with a molecular weight of 136 kDa and a sedimentation coefficient of 6.3 S. As a template, B. m. NPV polymerase prefers polydeoxynucleotide poly(dA) with a primer (dT)io and is inactive when using poly(A). Partially purified B. m. NPV polymerase is active on the single-standed circular phage M13 DNA in the absence of a primer. The ability to utilize phage M13 DNA as a template is due to the presence of a Mg2+-dependent endonuclease specific to double-stranded DNA in the preparations of B. m. NPV polymerase. The endonuclease exists in the B. m. NPV polymerase preparations after ammonium sulphate fractionation, phosphocellulose and hydroxyapatite chromatography but may be separated from B. m. NPV polymerase by glycerol gradient ultracentrifugation in the presence of 200 rnM potassium phosphate. At the lower salt concentrations B. m. NPV polymerase and the endonuclease reveal a tendency to aggregation.
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References

[1] Miller LK, Jewell JE, Browne D. Baculovirus induction of a DNA polymerase. J Virol. 1981;40(1):305-8.
[2] Wang X, Kelly DC. Baculovirus replication: purification and identification of the Trichoplusia ni nuclear polyhedrosis virus-induced DNA polymerase. J Gen Virol. 1983; 64(10):2229-2236.
[3] Zinder ND, Boeke JD. The filamentous phage (Ff) as vectors for recombinant DNA--a review. Gene. 1982;19(1):1-10.
[4] Zasloff M, Ginder GD, Felsenfeld G. A new method for the purification and identification of covalently closed circular DNA molcules. Nucleic Acids Res. 1978;5(4):1139-52.
[5] Onodera K, Komano T, Himeno M, Sakai F. The nucleic acid of nuclear-polyhedrosis virus of the silkworm. J Mol Biol. 1965;13(2):532-9.
[6] Mikhailov VS, Gulyamov DB. Changes in DNA polymerase alpha, beta, gamma activities during early development of the teleost fish Misgurnus fossilis (loach). Eur J Biochem. 1983;135(2):303-6.
[7] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[8] Oakley BR, Kirsch DR, Morris NR. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem. 1980;105(2):361-3.
[9] Mikhailov VS, Guliamov DB. Isolation of two forms of DNA polymerase alpha from roe of loach. Physico-chemical properties of the isoenzymes. Biokhimiia. 1983;48(9):1530-7.
[10] Ryndich AV, Sutugina LP, Kavsan VM etc. DNA polymerase activity of nuclear polyhedrosis virus large Wax moth. Dokl AN SSSR ser B, 1975; (4):347-349.
[11] Mikhailov B, Atayeva DO, Marlyev KA, Kullyev PK. Isolation of the replication complex comprising a DNA polymerase ? primase and a DNA of the silkworm silkworm Bombyx mori. Dokl AN SSSR. 1984; 275(2):502-505.