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Bacteriophage fd gene-2 protein. Processing of phage fd viral strands replicated by phage T7 enzymes

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Harth,  Günter
Max Planck Institute for Medical Research, Max Planck Society;

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Bäumel,  Irmtraud
Max Planck Institute for Medical Research, Max Planck Society;

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Meyer,  Thomas F.
Max Planck Institute for Medical Research, Max Planck Society;

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Geider,  Klaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Research Group Prof. Dr. Geider, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Harth, G., Bäumel, I., Meyer, T. F., & Geider, K. (1981). Bacteriophage fd gene-2 protein. Processing of phage fd viral strands replicated by phage T7 enzymes. European Journal of Biochemistry, 119(3), 663-668. doi:10.1111/j.1432-1033.1981.tb05659.x.


Cite as: https://hdl.handle.net/21.11116/0000-0004-F0B9-C
Abstract
Bacteriophage T7 gene 4 protein and DNA polymerase of the phage were used to study the viral strand synthesis of bacteriophage fd in vitro. Cleavage of supercoiled phage fd replicative form (RF) by fd gene 2 protein produced a nick at a specific site in the viral strand. The cleaved double-stranded DNA was unwound by T7 gene 4 protein and T7 DNA polymerase and the 3' end of the nicked strand simultaneously extended according to the rolling circle mechanism. After a complete round of DNA synthesis fd gene 2 protein cleaved the viral strand presumably at the same site, where the endonuclease cuts fd RF I, and subsequently sealed the single-stranded linear DNA into a circle. The reaction products were analyzed by velocity sedimentation, gel electrophoresis and electron microscopy. Most of the single-stranded DNA synthesized was circular. No host proteins were required for the formation of the single-stranded circles. Strand switching of the T7 DNA polymerase indicated by double-stranded tails of the rolling circle structures reduced the yield of viral single-stranded circles in this enzyme system.