Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I

Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements

https://mmbr.asm.org/content/mmbr/47/1/1.full.pdf

Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles.

Covalently closed circular duplex DNA’s are now known to be widespread among living organisms. This DNA structure, originally identified in polyoma viral DNA,1’2 has been assigned to the mitochondrial DNA’s in ox3 and sheep heart,4 in mouse and chicken liver,3 and in unfertilized sea urchin egg.5 The animal viral DNA’s—polyoma, SV40,6 rabbit7 and human8 papilloma—the intracellular forms of the bacterial viral DNA’s—φX174,9, 10 lambda,11, 12 M13,13 and P2214—and a bacterial plasmid DNA, the colicinogenic factor E2,15 have all been shown to exist as closed circular duplexes. Other mitochondrial DNA’s16, 17 and a portion of the DNA from boar sperm18 have been reported to be circular, but as yet have not been shown to be covalently closed.

A dye-buoyant-density method for the detection and isolation of closed circular duplex DNA: the closed circular DNA in HeLa cells.

https://www.cell.com/cell/pdf/0092-8674(78)90039-9.pdf

How do eucaryotic ribosomes select initiation regions in messenger RNA

Novel Intra-cellular Forms of Lambda DNA

Vegetative bacteriophage λ DNA: II. Physical characterization and replication

RNase III had no positive effect on the translation of bacteriophage T7 lysozyme mRNA in vivo or in vitro. The time of appearance and quanity of lysozyme in T7-infected E. coli BL107, an RNase III- strain, and T7-infected E. coli BL15, a nearly isogenic RNase III+ strain, were indistinguishable. Nearly identical patterns of lysozyme mRNA activity were obtained when RNA extracted at different times after infection of RNase III+ and RNase III- hosts was translated in cell-free extracts of E. coli containing or lacking RNase III. Exposure of RNA extracted from T7-infected E. coli BL107 (RNase III-) to purified RNase III did not increase the lysozyme mRNA activity of this RNA. The only result that implied that RNase III has a differential effect on the translatability of the lysozyme mRNA was the translation of fractionaed RNA from T7-infected E. coli BL107. Translation of the smallest and largest lysozyme messages, 0.33 x 10(6) and 4 x 10(6) to 5 x 10(6) daltons, was the most inefficient in RNase III- cell-free extracts as compared to RNase III+ cell-free translation. The translation of the most abundant, medium-sized lysozyme mRNA between 0.9 x 10(6) and 1.5 x 10(6) daltons was the least affected by the absence of RNase III. The existence of a lag between the appearance of lysozyme mRNA and the appearance of lysozyme in T7 infection was confirmed. In these studies a very rapid method of RNA extraction was used, eliminating the possibility of continued RNA transcription during cell collection and RNA extraction. With this method of analysis, the length of the lag period was established at about 3 min. The possibility that RNase III is the controlling element of the lag period was eliminated by these investigations.

Effect of RNase III on efficiency of translation of bacteriophage T7 lysozyme mRNA.

http://www.jbc.org/content/240/3/1274.full.pdf

Elton T. Young

Papers

Novel Intra-cellular Forms of Lambda DNA

Vegetative bacteriophage λ DNA: II. Physical characterization and replication

Effect of RNase III on efficiency of translation of bacteriophage T7 lysozyme mRNA.

A comparison of the initial actions of spleen deoxyribonuclease and pancreatic deoxyribonuclease.

Vegetative bacteriophage λ DNA: I. Infectiv in a spheroplast assay☆