Pseudovirulent mutants of λb221poriCasnA resulting from mutations in or near oriC, the E. coli origin of DNA replication

1980 ◽  
Vol 178 (2) ◽  
pp. 391-396 ◽  
Author(s):  
Larry Soll
Keyword(s):  
Dna Replication ◽  
E Coli ◽  
Origin Of Dna Replication

scholarly journals Expression, purification and characterization of the Spodoptera littoralis nucleopolyhedrovirus (SpliNPV) DNA polymerase and interaction with the SpliNPV non-hr origin of DNA replication

2001 ◽  
Vol 82 (7) ◽  
pp. 1767-1776 ◽  
Author(s):  
Jianhe Huang ◽  
David B. Levin
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Spodoptera Littoralis ◽  
Expression System ◽  
Functional Characterization ◽  
Eukaryotic Expression ◽  
Replication Assay ◽  
E Coli ◽  
Origin Of Dna Replication

The DNA polymerase from Spodoptera littoralis nucleopolyhedrovirus (SpliNPV) was expressed in, and purified from, prokaryotic and eukaryotic expression systems. While less protein was obtained from the E. coli expression system, SpliNPV DNAPOL purified from E. coli displayed similar biochemical characteristics to DNAPOL expressed in, and subsequently purified from, insect cells (Sf9) using a baculovirus expression system. Biochemical analyses suggested that the DNA polymerase and the 3′–5′ exonuclease activities are intrinsic to the protein. Deletion of the first 80 amino acid residues from the N terminus of the DNAPOL affected neither the DNA polymerase nor the exonuclease activities of the enzyme. Replication products from single-stranded M13 DNA demonstrated that the DNA synthesis activity of SpliNPV DNAPOL is highly processive. Transient expression assays with a set of deletion clones containing the putative SpliNPV non-hr origin of DNA replication permitted functional characterization of sequence elements within the origin fragment. Purified SpliNPV DNAPOL stimulated origin-dependent DNA replication in a cell-free replication assay.

Proximity of deoxyadenylic-thymidylic acid clusters to origin of DNA replication in E. coli 15T− cells

Nature ◽  
1975 ◽  
Vol 255 (5505) ◽  
pp. 252-253 ◽  
Author(s):  
BETTY B. BARIL ◽  
H. KUBINSKI
Keyword(s):  
Dna Replication ◽  
E Coli ◽  
Origin Of Dna Replication

On the localization of the origin of DNA replication in E. coli

1977 ◽  
Vol 64 (4) ◽  
pp. 747-760
Author(s):  
Samuel Litwin ◽  
Neville R. Kallenbach
Keyword(s):  
Dna Replication ◽  
E Coli ◽  
Origin Of Dna Replication

Replication of Bacteriophage 186 DNA

1972 ◽  
Vol 30 ◽  
pp. 194-195
Author(s):  
Dhruba K. Chattoraj ◽  
Ross B. Inman
Keyword(s):  
Electron Microscopy ◽  
Dna Replication ◽  
Frame Of Reference ◽  
Dna Molecules ◽  
E Coli ◽  
Phage Dna ◽  
Partial Denaturation

Electron microscopy of replicating intermediates has been quite useful in understanding the mechanism of DNA replication in DNA molecules of bacteriophage, mitochondria and plasmids. The use of partial denaturation mapping has made the tool more powerful by providing a frame of reference by which the position of the replicating forks in bacteriophage DNA can be determined on the circular replicating molecules. This provided an easy means to find the origin and direction of replication in λ and P2 phage DNA molecules. DNA of temperate E. coli phage 186 was found to have an unique denaturation map and encouraged us to look into its mode of replication.

Cellular proteins bind to the downstream component of the lytic origin of DNA replication of Epstein-Barr virus.

1995 ◽  
Vol 69 (3) ◽  
pp. 1878-1886 ◽  
Author(s):  
H Gruffat ◽  
O Renner ◽  
D Pich ◽  
W Hammerschmidt
Keyword(s):  
Dna Replication ◽  
Epstein Barr Virus ◽  
Cellular Proteins ◽  
Barr Virus ◽  
Origin Of Dna Replication ◽  
Epstein Barr

scholarly journals E. coli primase and DNA polymerase III holoenzyme are able to bind concurrently to a primed template during DNA replication

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Andrea Bogutzki ◽  
Natalie Naue ◽  
Lidia Litz ◽  
Andreas Pich ◽  
Ute Curth
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Protein Interactions ◽  
Dna Polymerase Iii ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
E Coli ◽  
Polymerase Iii ◽  
C Terminus ◽  
Pol Iii

Abstract During DNA replication in E. coli, a switch between DnaG primase and DNA polymerase III holoenzyme (pol III) activities has to occur every time when the synthesis of a new Okazaki fragment starts. As both primase and the χ subunit of pol III interact with the highly conserved C-terminus of single-stranded DNA-binding protein (SSB), it had been proposed that the binding of both proteins to SSB is mutually exclusive. Using a replication system containing the origin of replication of the single-stranded DNA phage G4 (G4ori) saturated with SSB, we tested whether DnaG and pol III can bind concurrently to the primed template. We found that the addition of pol III does not lead to a displacement of primase, but to the formation of higher complexes. Even pol III-mediated primer elongation by one or several DNA nucleotides does not result in the dissociation of DnaG. About 10 nucleotides have to be added in order to displace one of the two primase molecules bound to SSB-saturated G4ori. The concurrent binding of primase and pol III is highly plausible, since even the SSB tetramer situated directly next to the 3′-terminus of the primer provides four C-termini for protein-protein interactions.

scholarly journals Phosphorylation-dependent interaction of adenovirus preterminal protein with the viral origin of DNA replication.

1994 ◽  
Vol 269 (3) ◽  
pp. 2189-2196
Author(s):  
J. Kusukawa ◽  
M. Ramachandra ◽  
R. Nakano ◽  
R. Padmanabhan
Keyword(s):  
Dna Replication ◽  
Viral Origin ◽  
Origin Of Dna Replication ◽  
Dependent Interaction

scholarly journals The replication machinery of LUCA: common origin of DNA replication and transcription

BMC Biology ◽  
2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Eugene V. Koonin ◽  
Mart Krupovic ◽  
Sonoko Ishino ◽  
Yoshizumi Ishino
Keyword(s):  
Dna Replication ◽  
Common Origin ◽  
Replication Machinery ◽  
Origin Of Dna Replication
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