The mechanism of replication of øX174 DNA

Eisenberg, Shlomo; Harbers, Barbara; Hours, Christian; Denhardt, David T.

doi:10.1016/s0022-2836(75)80162-8

Cited by 77 publications

(24 citation statements)

References 32 publications

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“…The initiation [77,78] and termination [77] sites of viral strand synthesis have been visualized on these replicative intermediates and these sites are in full agreement with the biochemical data [56,62,79]. The initiation of complementary strand synthesis on the replicative intermediates at many different although not random sites [77] has also confirmed earlier biochemical experiments [80,81].…”

Section: Ivc Complementary Strand Synthesis During Rf Dna Replicationsupporting

confidence: 86%

DNA replication of single-stranded Escherichia coli DNA phages

Baas

1985

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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Section: Ivc Complementary Strand Synthesis During Rf Dna Replicationsupporting

confidence: 86%

DNA replication of single-stranded Escherichia coli DNA phages

Baas

1985

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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“…4). It is noticeable that the C6,T pyrimidine tract (4285-4291) that was observed (29) (24) and from the detailed restriction cleavage map derived from DNA sequencing studies (G. N. Godson and J. C. Fiddes, unpublished data). The two scales are in base pairs, with arbitrary zero points.…”

Section: Resultsmentioning

confidence: 97%

Nucleotide sequences of the separate origins of synthesis of bacteriophage G4 viral and complementary DNA strands.

Fiddes¹,

Barrell²,

Godson³

1978

Proc. Natl. Acad. Sci. U.S.A.

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Bacteriophage G4 has physically separated origins of synthesis of its viral and complementary DNA strands. Chain termination and "plus and minus" DNA sequencing methods have been used to obtain the nucleotide sequence of these two origins. The unique origin at which the complementary DNA strand is initiated has been located in the untranslated region between genes F and G. This sequence, which has considerable secondary structure DNA Sequence Analysis. The plus and minus procedure (21) was used as described by Barrell (22), and the chain termination method of DNA sequence analysis was that of Sanger et al. (23). RESULTS AND DISCUSSIONSequence of the G4 Origin of Viral DNA Strand Synthesis. The origin of G4 viral strand synthesis has been located in the restriction enzyme fragment Hae III 2a (4, 11-13). On the aligned G4 and OX 174 restriction enzyme cleavage map (Fig. 1) G4 fragment Hae III 2a covers OX 174 fragment Hae III 6b, which is known to contain the origin of OX174 viral DNA strand synthesis (14,26,27). The XX174 viral strand origin has recently been located precisely on the complete OX174 DNA sequence of Sanger et al. (25) by the observation that the OX174 cistron A protein cleaves the viral strand of OX174 RF I DNA between nucleotides 4297 (G) and 4298 (A) (28). The nucleotide sequence of the corresponding region of G4 DNA has now been determined using the chain termination method of Sanger et al. (23).The appropriate restriction endonuclease fragments to use as primers were selected from an examination of the G4 restriction enzyme map (see Fig. 2 for the map of this region). The autoradiographs of the sequencing gels obtained when Hha I fragment 6 and Alu I fragment 4 were used as primers with viral strand DNA as template are shown in Fig. 3 a and b. These two priming sites are located downstream of the origin. Also shown (Fig. Sc) is the autoradiograph of a priming using a Hae III-generated subproduct of Taq I fragment 8 (Taq I V8) with complementary strand DNA as template. This priming site is located upstream of the origin.Withone region of ambiguity, a sequence 72 nucleotides long Abbreviation: RF, replicative form.

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“…and M13 DNA were prepared as described (13); calf thymus DNA was from Calbiochem; P22 DNA, P22 [3H]DNA, X precA99 DNA, and E. coli RNA polymerase were from K.…”

Section: Methodsmentioning

confidence: 99%

Novel histone H2A-like protein of escherichia coli.

Hübscher¹,

Lutz²,

Kornberg³

1980

Proc. Natl. Acad. Sci. U.S.A.

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ABSIRACT A histone-like protein (H) from Escherichia coli has been purified to more than 98% homogeneity by using its capacity to inhibit DNA functions. H protein behaves as a dimer of 28,000-dalton subunits. The histone H2A-like properties of H protein are: (i) The Escherichia coli chromosome can be isolated in a folded, condensed, supercoiled form (1-4). A search for histone-like proteins in E. coli and other prokaryotes has yielded several low molecular weight, basic, DNA-binding proteins that resemble eukaryotic histones (5)(6)(7)(8)(9). A pair of HU proteins, also known as protein 2, are near 9000 daltons in size and resemble the eukaryotic histones in (i) binding to DNA, (ii) having an amino acid composition like that of histone H2B, (ii) being heat and acid stable, and (iv) forming a nucleosome-like structure with duplex DNA (9, 10). In addition, a histone-like protein of 17,000 daltons in E. colh (8) and a low molecular weight protein in thermophilic mycoplasma (Thermoplasma acidophilum) similar to histone H4 (11) have been described.In the course of purifying E. colh replication proteins (12) and possible regulatory factors, we encountered an inhibitor that appears to be a novel histone-like protein, provisionally called H protein, that shows immunological crossreactivity with the eukaryotic histone H2A. As a result of tight binding to DNA, H protein inhibits DNA functioning as a template for polymerases, as a substrate for nuclease and topoisomerase, and as an effector for ATPase; it also activates annealing of homologous single strands. H protein may have a significant role in the structure and function of the E. coli chromosome. MATERIALS AND METHODSNucleic Acids, Nucleotides, Enzymes, and Proteins. kX174and M13 DNA were prepared as described (13) sl of 50 mM NaOAc, pH 4.6/150 mM NaCl/1 mM Zn(OAc)2 was added, followed by 100 units of S1 nuclease. Incubation was at 370C for 30 min. After addition of calf thymus ss DNA to 150 ,ug/ml and precipitation with an equal volume of 10% (wt/vol) trichloroacetic acid, the acid-insoluble radioactive material was filtered and measured as described (15). Under these conditions, in the absence of H protein, 3% of the input DNA was acid insoluble (S1 nuclease resistant). The acid-insoluble radioactivity of native P22 [3H]DNA was taken as the 100% S1 nucleasbresistant value.Antisera and Enzyme-Linked Immunosorbent Assay (ELISA). Antisera against calf thymus histones HI, H2A, and H2B were prepared in rabbits by R. Sperling and M: Bustin as described (17), and their specificity was measured by complement fixation (18).

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The mechanism of replication of øX174 DNA

Cited by 77 publications

References 32 publications

DNA replication of single-stranded Escherichia coli DNA phages

DNA replication of single-stranded Escherichia coli DNA phages

Nucleotide sequences of the separate origins of synthesis of bacteriophage G4 viral and complementary DNA strands.

Novel histone H2A-like protein of escherichia coli.

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