Escherichia coli deoxyribonucleic acid synthesis mutants: their effect upon bacteriophage P2 and satellite bacteriophage P4 deoxyribonucleic acid synthesis

Bowden, Donald W.; Twersky, R S; Calendar, Richard

doi:10.1128/jb.124.1.167-175.1975

Cited by 47 publications

(15 citation statements)

References 36 publications

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“…The following strains were used: E. coli C recA171 (recA, rif5, 0Xs); E. coli TCC122 (WXs); E. coli HF4712 (0XS, SupAUG); E. coli LD311 (uvrA, thyA, endl, dnaBts, 0Xs) (17); E. coli LD332 (uvrA, thyA, endl, dnaCts, OXs) (17), and E. coli C2309 (uvrA, thyA, dnaGts, 0Xs) (18). The phages OX am3 and G4 amE2 are lysis-defective amber mutants in gene E of bacteriophage 0X174 and G4, respectively (19,20).…”

Section: Bacterial Strains and Phagesmentioning

confidence: 99%

Initiation signals for complementary strand DNA synthesis on single-stranded plasmid DNA

et al. 1983

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The bacteriophage 0X174 origin for (+) strand DNA synthesis, when inserted in a plasmid, is in vivo a substrate for the initiator A protein, that is produced by infecting phages. The result of this interaction is the packaging of single-stranded plasmid DNA into preformed phage coats. These plasmid particles can transduce 0X-sensitive cells; however, the transduction efficiency depends strongly on the presence in the packaged DNA strand of an initiation signal for complementary strand DNA synthesis. A plasmid with the complementary (-) strand origin of 0X inserted in the same strand as the viral (+) origin transduces 50-100 times more efficient than the same plasmid without the (-) origin of 0X. The transduction efficiency of such a particle is comparable to the infection efficiency of the phage particle. It is shown that in this system the 0X (-) origin can be replaced by the complementary strand origins of the bacteriophages G4 and M13. We have used this system to isolate sequences, from E. coli plasmids (pACYC177, CloDF13, miniF and OriC) and from the E. coli chromosome that can function as initiation signals for the conversion of single-stranded plasmid DNA to double-stranded DNA. All isolated origins were found to be dependent for their activity on the dnaB, dnaC and dnaG proteins. We conclude that these signals were all primosome-dependent origins and that primosome priming is the major mechanism for initiation of the lagging strand DNA synthesis in E. coli. The assembly of the primosome depends on the sequence-specific interaction of the n' protein with single-stranded DNA. We have used the isolated sequences to deduce a consensus recognition sequence for the n' protein. The role of a possible secondary structure in this sequence is discussed.

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Section: Bacterial Strains and Phagesmentioning

confidence: 99%

Initiation signals for complementary strand DNA synthesis on single-stranded plasmid DNA

et al. 1983

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“…Besides the requirement for their respective A protein, 0X174 and P2 require the host functions of genes dnaE (a-subunit of polII), dnaB (helicase), dnaG (primase) and rep (helicase) (25,26). In contrast to both 0X174 and 186, P2 is independent of the dnaC gene function (25,27), and it has been hypothesized that the P2 B protein is a DnaC analogue (4, 10). However, the P2 B protein is essential for phage DNA replication (3), but for the replication of a P2 mini-chromosome (11).…”

Section: Discussionmentioning

confidence: 99%

Studies of bacteriophage P2 DNA replication: localization of the cleavage site of the A protein

Liu

Haggård‐Ljungquist

1994

Nucl Acids Res

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Bacteriophage P2 replicates via a modified rolling circle-type of mechanism, where the P2 A protein acts as an initiator of the replication by inducing a single-stranded cut at the origin of replication (ori). The exact location of the cut induced by the A protein in vivo is determined in this report by: (i) restriction analysis; (ii) DNA sequence analysis; and (iii) primer extensions. It is located 89.2% from the left end of the P2 genome, which is within the coding part of the A gene, in a region devoid of secondary structures. The A gene has been cloned into an expression vector, and the A protein has been purified. The purified A protein does not bind to double-stranded ori containing DNA, but it cleaves single-stranded ori containing DNA, which indicates that a special DNA structure and/or protein is required to make the ori accessible for the A protein.

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“…Barrett et al [13] have described a rifampicin-resistant RNA polymerase activity of gp~ on several synthetic DNA templates. Since P4 replicates in dnaGts mutants at non-permissive temperatures, the phage was thought to be independent of cellular priming systems [8]. Thus, it was proposed that gp~x possesses primase activity.…”

Section: Primase Activity Of Gpo~mentioning

confidence: 99%

“…Proteins DnaA, DnaB, DnaC, DnaG, Rep and RNA polymerase are dispensable. These early observations made in the Calendar laboratory in the midseventies, suggested P4 replication to be unique among temperate phages in terms of recruiting only a few host replication proteins [8], i.e. the elongation machinery.…”

Section: Introductionmentioning

confidence: 99%

Bacteriophage P4 DNA replication

Ziegelin

1995

FEMS Microbiology Reviews

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Replication of satellite phage P4 of Escherichia coli is dependent on three phage-encoded elements: the origin (ori), a cis replication element (crr), and the product of the alpha gene, gp alpha. In P4 replication is origin-specific resulting in monomeric form I DNA. DNA synthesis requires chromosomally encoded proteins DNA polymerase III holoenzyme, SSB, DNA gyrase and probably topoisomerase I; host-encoded initiation and priming functions are dispensable. The alpha protein is multifunctional in P4 replication, combining three activities in a single polypeptide chain. First, the protein complexes specifically with type I repeats at ori and crr. Second, the helicase activity associated with gp alpha unwinds DNA with 3'--> 5' polarity. Third, the primase activity results in the synthesis of RNA primers. Defined sequence motifs in gp alpha correlate with the helicase and primase activities which are arranged in distinct, separable domains. Primase activity is associated with the N-terminal half of the protein, ori/crr binding with the C-terminal portion. A model for the initiation mechanism of P4 replication which resembles that of mammalian simian virus 40 is discussed.

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Escherichia coli deoxyribonucleic acid synthesis mutants: their effect upon bacteriophage P2 and satellite bacteriophage P4 deoxyribonucleic acid synthesis

Cited by 47 publications

References 36 publications

Initiation signals for complementary strand DNA synthesis on single-stranded plasmid DNA

Initiation signals for complementary strand DNA synthesis on single-stranded plasmid DNA

Studies of bacteriophage P2 DNA replication: localization of the cleavage site of the A protein

Bacteriophage P4 DNA replication

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