Results 101 to 110 of about 2,219 (132)
In bacterial DNA replication, the initiator protein DnaA binds to the multiple DnaA box sequences located at oriC to facilitate the unwinding of duplex DNA strands. The cyanobacterium Synechococcus elongatus PCC 7942, which contains multiple chromosomal copies per cell, has DnaA box (like sequences around the oriC region, which is located upstream of ...
Ryudo Ohbayashi, Satoru Watanabe
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Insights into the Quality of DnaA Boxes and Their Cooperativity
Journal of Molecular Biology, 2006Plasmids carrying the mioC promoter region with its two DnaA boxes are as efficient in titration of DnaA protein as plasmids carrying a replication-inactivated oriC region with its five DnaA boxes. The two DnaA boxes upstream of the mioC promoter were mutated in various ways to study the cooperativity between the DnaA boxes, and to study in vivo the in
Bjarke Bak Christensen +2 more
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Titration of DnaA protein by oriC DnaA‐boxes increases dnaA gene expression in Escherichia coli.
Binding of the DnaA protein to its binding sites, the DnaA-boxes (TTATCCACA), was measured by a simple physiological approach. The presence of extra DnaA-boxes in growing cells leads to a derepression of dnaA gene expression, measured as beta-galactosidase activity of a dnaA-lacZ fusion polypeptide.
Tove Atlung, Flemming G Hansen
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Cellular and Molecular Life Sciences, 2003
DnaA protein binds specifically to a 9-base- pair motif called the DnaA box. Domain IV comprises 94 amino acid residues and is required for DNA binding. Using nuclear magnetic resonance analysis, we investigated the interaction between DnaA domain IV and both a DnaA box and a non-specific oligonucleotide that has a reduced affinity for DnaA. The 1H-15N
T Ohmura
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DnaA protein binds specifically to a 9-base- pair motif called the DnaA box. Domain IV comprises 94 amino acid residues and is required for DNA binding. Using nuclear magnetic resonance analysis, we investigated the interaction between DnaA domain IV and both a DnaA box and a non-specific oligonucleotide that has a reduced affinity for DnaA. The 1H-15N
T Ohmura
exaly +3 more sources
DnaA protein binding to individual DnaA boxes in the Escherichia coli replication origin, oriC [PDF]
The formation of nucleoprotein complexes between the Escherichia coli initiator protein DnaA and the replication origin oriC was analysed in vitro by band-shift assays and electron microscopy. DnaA protein binds equally well to linear and supercoiled oriC substrates as revealed by analysis of the binding preference to individual DnaA boxes (9-mer ...
Christoph Weigel +2 more
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Trigger factor interacts with DnaA protein to stimulate its interaction with DnaA box
Korean Journal of Biological Sciences, 2003While screening proteins that interact with DnaA protein, the initiator protein for Escherichia coli chromosomal DNA replication, we found a 52‐kD sized protein which bound to DnaA protein in a salt‐dependent manner. This protein was identified as trigger factor, a ribosome‐associated peptidyl‐prolyl‐cis/trans isomerase with chaperone activity. Trigger
Sukhyun Kang, Jae Bum Kim, Joo Seok Han
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The presence of two DnaA-binding sequences is required for an efficient interaction of the Escherichia coli DnaA protein with each particular weak DnaA box region [PDF]
Using an electron microscopic method for visualizing interactions of the Escherichia coli DnaA protein with weak DnaA-binding DNA sequences, we found that DnaA binds effectively to two separated weak DnaA box regions located on the same DNA fragment. As expected, no DnaA-DNA interactions were detected when both DnaA box regions were mutagenized to the ...
Agnieszka Szalewska-Pałasz +2 more
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Molecular Microbiology, 1991
SummaryDnaA protein (a trans‐acting element) and its binding sequence, DnaA‐box: (a cis‐acting element) are two elements essential for the initiation of chromosomal replication in Escherichia coli and other enteric bacteria. Recently these two elements have been found to be conserved in three Gram‐positive bacteria (Bacillus subtilis, Micrococcus ...
H, Yoshikawa, N, Ogasawara
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SummaryDnaA protein (a trans‐acting element) and its binding sequence, DnaA‐box: (a cis‐acting element) are two elements essential for the initiation of chromosomal replication in Escherichia coli and other enteric bacteria. Recently these two elements have been found to be conserved in three Gram‐positive bacteria (Bacillus subtilis, Micrococcus ...
H, Yoshikawa, N, Ogasawara
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Gene, 1992
We have previously shown that the dnaA gene and the DnaA-box region were conserved in bacteria representative of all three major branches of the eubacterial phylogenic tree: high G + C Gram+, low-G + C Gram+ and Gram-. In the present work, we determined the structure of the dnaA region of Mycoplasma capricolum and found that the dnaA gene and at least ...
M Q, Fujita, H, Yoshikawa, N, Ogasawara
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We have previously shown that the dnaA gene and the DnaA-box region were conserved in bacteria representative of all three major branches of the eubacterial phylogenic tree: high G + C Gram+, low-G + C Gram+ and Gram-. In the present work, we determined the structure of the dnaA region of Mycoplasma capricolum and found that the dnaA gene and at least ...
M Q, Fujita, H, Yoshikawa, N, Ogasawara
openaire +2 more sources
European Journal of Biochemistry, 1995
The ABC primosome is assembled from DnaA, DnaB and DnaC proteins at a stem-and-loop structure containing a dnaA box within its stem (A site), and catalyses primer RNA synthesis for DNA chain elongation. The DnaA protein can bind to the A site and the A-site-DnaA-protein complex can be isolated by gel-filtration chromatography in the absence of ...
H, Masai, K I, Arai
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The ABC primosome is assembled from DnaA, DnaB and DnaC proteins at a stem-and-loop structure containing a dnaA box within its stem (A site), and catalyses primer RNA synthesis for DNA chain elongation. The DnaA protein can bind to the A site and the A-site-DnaA-protein complex can be isolated by gel-filtration chromatography in the absence of ...
H, Masai, K I, Arai
openaire +2 more sources

