Replication of plasmids in gram-negative bacteria
U Kües, U Stahl - Microbiological reviews, 1989 - Am Soc Microbiol
Replication of plasmid deoxyribonucleic acid (DNA) is dependent on three stages: initiation,
elongation, and termination. The first stage, initiation, depends on plasmid-encoded …
elongation, and termination. The first stage, initiation, depends on plasmid-encoded …
Replication of coliphage lambda DNA
K Taylor, G Wçgrzyn - FEMS microbiology reviews, 1995 - academic.oup.com
A general scheme of λ phage and plasmid DNA replication in Escherichia coli is presented,
and results of in vivo experiments from the authors' laboratory are superimposed. The …
and results of in vivo experiments from the authors' laboratory are superimposed. The …
Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication.
K Liberek, C Georgopoulos… - Proceedings of the …, 1988 - National Acad Sciences
We examined the role of two Escherichia coli heat shock proteins, the dnaK and dnaJ gene
products, during the initiation of lambda dv DNA replication in vitro. Using 14C-labeled …
products, during the initiation of lambda dv DNA replication in vitro. Using 14C-labeled …
The dnaB-dnaC replication protein complex of Escherichia coli: I. Formation and properties
E Wahle, RS Lasken, A Kornberg - Journal of Biological Chemistry, 1989 - ASBMB
The complex formed between the dnaB and dnaC replication proteins of Escherichia coli is
stabilized by ATP binding to dnaC. The dnaB 6-dnaC 6-ATP 6 complex can be maintained …
stabilized by ATP binding to dnaC. The dnaB 6-dnaC 6-ATP 6 complex can be maintained …
[HTML][HTML] Primase directs the release of DnaC from DnaB
M Makowska-Grzyska, JM Kaguni - Molecular cell, 2010 - cell.com
Summary An AAA+ ATPase, DnaC, delivers DnaB helicase at the E. coli chromosomal origin
by a poorly understood process. This report shows that mutant proteins bearing alanine …
by a poorly understood process. This report shows that mutant proteins bearing alanine …
[HTML][HTML] Host virus interactions in the initiation of bacteriophage lambda DNA replication. Recruitment of Escherichia coli DnaB helicase by lambda P replication …
JB Mallory, C Alfano, R McMacken - Journal of Biological Chemistry, 1990 - Elsevier
The bacteriophage lambda P protein promoters replication of the phage chromosome by
recruiting a key component of the cellular replication machinery to the viral origin …
recruiting a key component of the cellular replication machinery to the viral origin …
ATPase switches controlling DNA replication initiation
DG Lee, SP Bell - Current opinion in cell biology, 2000 - Elsevier
Proteins that bind and hydrolyze ATP are frequently involved in the early steps of DNA
replication. Recent studies of Saccharomyces cerevisiae suggest that two members of the …
replication. Recent studies of Saccharomyces cerevisiae suggest that two members of the …
[HTML][HTML] Crystal structure of the N-terminal domain of the DnaB hexameric helicase
Abstract Background: The hexameric helicase DnaB unwinds the DNA duplex at the
Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both …
Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both …
[HTML][HTML] Emerging heterogeneous compartments by viruses in single bacterial cells
Spatial organization of biological processes allows for variability in molecular outcomes and
coordinated development. Here, we investigate how organization underpins phage lambda …
coordinated development. Here, we investigate how organization underpins phage lambda …
Specialized nucleoprotein structures at the origin of replication of bacteriophage λ: protein association and disassociation reactions responsible for localized initiation …
M Dodson, R McMacken, H Echols - Journal of Biological Chemistry, 1989 - Elsevier
Binding of the O protein of phage λ to the replication origin (oriλ) results in the formation of
an organized nucleoprotein structure termed the O-some. The O-some serves to localize …
an organized nucleoprotein structure termed the O-some. The O-some serves to localize …