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Howard A. Nash
National Institutes of Health
Citations
4748
H-index
34
Publications 73
Most Citations
Martin Gellert57
Estimated H-index: 57
(National Institutes of Health),
Kiyoshi Mizuuchi28
Estimated H-index: 28
(Laboratory of Molecular Biology),
M H O'Dea12
Estimated H-index: 12
(National Institutes of Health)
... (1 others)
Abstract Relaxed closed-circular DNA is converted to negatively supercoiled DNA by DNA gyrase. This enzyme has been purified from Escherichia coli cells. The reaction requires ATP and Mg++ and is stimulated by spermidine. The enzyme acts equally well on relaxed closed-circular colicin E1, phage lambda, and simian virus 40 DNA. The final superhelix density of the DNA can be considerably greater tha...
Cited 661 Source Cite this paper
2016 in Cell [IF: 30.41]
Phoebe A. Rice35
Estimated H-index: 35
(National Institutes of Health),
Shu-wei Yang1
Estimated H-index: 1
(National Institutes of Health),
Kiyoshi Mizuuchi39
Estimated H-index: 39
(National Institutes of Health)
... (1 others)
Abstract Integration host factor (IHF) is a small heterodimeric protein that specifically binds to DNA and functions as an architectural factor in many cellular processes in prokaryotes. Here, we report the crystal structure of IHF complexed with 35 bp of DNA. The DNA is wrapped around the protein and bent by >160°, thus reversing the direction of the helix axis within a very short distance. Much ...
Ref 63Cited 564 Source Cite this paper
2016 in Cell [IF: 30.41]
Nancy L. Craig46
Estimated H-index: 46
(National Institutes of Health),
Howard A. Nash34
Estimated H-index: 34
(National Institutes of Health)
Abstract E. coli integration host factor (IHF) both participates directly in phage lambda site-specific recombination and regulates the expression of phage and bacterial genes. Using protection from nuclease and chemical attack as an assay, we examined the interaction of IHF with DNA. We found that IHF is a specific DNA binding protein that interacts with three distinct segments of attP, the recom...
Ref 32Cited 269 Source Cite this paper
2016 in Science [IF: 37.20]
Jeffrey J. Pouliot6
Estimated H-index: 6
(National Institutes of Health),
Kevin C. Yao1
Estimated H-index: 1
(National Institutes of Health),
Carol A. Robertson2
Estimated H-index: 2
(National Institutes of Health)
... (1 others)
Covalent intermediates between topoisomerase I and DNA can become dead-end complexes that lead to cell death. Here, the isolation of the gene for an enzyme that can hydrolyze the bond between this protein and DNA is described. Enzyme-defective mutants of yeast are hypersensitive to treatments that increase the amount of covalent complexes, indicative of enzyme involvement in repair. The gene is co...
Ref 15Cited 268 Download Pdf Cite this paper
S W Yang1
Estimated H-index: 1
,
A B Burgin1
Estimated H-index: 1
,
B N Huizenga1
Estimated H-index: 1
... (3 others)
Abstract The covalent joining of topoisomerases to DNA is normally a transient step in the reaction cycle of these important enzymes. However, under a variety of circumstances, the covalent complex is converted to a long-lived or dead-end product that can result in chromosome breakage and cell death. We have discovered and partially purified an enzyme that specifically cleaves the chemical bond th...
Ref 2Cited 265 Download Pdf Cite this paper
2016 in Cell [IF: 30.41]
Chien-Chin Yang1
Estimated H-index: 1
(National Institutes of Health),
Howard A. Nash34
Estimated H-index: 34
(National Institutes of Health)
Abstract We have used two kinds of footprinting techniques, dimethylsulfate interference and hydroxyl radical protection, to explore the way that IHF recognizes its specific target sequences. Our results lead us to conclude that IHF recognizes DNA primarily through contacts with the minor groove, an unprecedented mode for a sequence-specific binding protein. We have also determined that, although ...
Ref 49Cited 203 Source Cite this paper
2016 in Nature [IF: 40.14]
Steven D. Goodman1
Estimated H-index: 1
,
Howard A. Nash34
Estimated H-index: 34
(National Institutes of Health)
An important question to be answered in these cases is whether bending of DNA is important per se or is merely a consequence of the way a particular protein binds to DNA. Here we report direct evidence form the bacteriophage lambda integration system that a bend introduced by a protein is intrinsically important. We find that a binding site for a specific recombination protein known to bend DNA ca...
Cited 159 Source Cite this paper
Chunyan Liu2
Estimated H-index: 2
(National Institutes of Health),
Jeffrey J. Pouliot6
Estimated H-index: 6
(National Institutes of Health),
Howard A. Nash34
Estimated H-index: 34
(National Institutes of Health)
Accidental or drug-induced interruption of the breakage and reunion cycle of eukaryotic topoisomerase I (Top1) yields complexes in which the active site tyrosine of the enzyme is covalently linked to the 3′ end of broken DNA. The enzyme tyrosyl-DNA phosphodiesterase (Tdp1) hydrolyzes this protein-DNA link and thus functions in the repair of covalent complexes, but genetic studies in yeast show tha...
Ref 43Cited 121 Download Pdf Cite this paper
2016 in Genes to Cells [IF: 1.99]
Jeffrey J. Pouliot6
Estimated H-index: 6
(National Institutes of Health),
Carol A. Robertson2
Estimated H-index: 2
(National Institutes of Health),
Howard A. Nash34
Estimated H-index: 34
(National Institutes of Health)
Background The covalent linkage between DNA and the active site tyrosine of topoisomerase I can be stabilized by chemotherapeutic agents, adjacent DNA lesions, or mutational defects in the topoisomerase itself. Following collision with a replication fork, the covalent complex can be converted to a double-strand break. Tdp1, an enzyme that can hydrolyse the bond between topoisomerase I and DNA, is ...
Ref 36Cited 117 Source Cite this paper
2016 in Cell [IF: 30.41]
Evelyne Richet2
Estimated H-index: 2
(National Institutes of Health),
Peter Abcarian2
Estimated H-index: 2
(National Institutes of Health),
Howard A. Nash34
Estimated H-index: 34
(National Institutes of Health)
Abstract During lambda integration, Int recombinase must specifically bind to and cut attachment sites on both the viral and host chromosomes. We show here by foot-printing and by a novel cleavage assay that the bacterial attachment site, att B, cannot stably bind Int in competition with other DNAs. Instead, during recombination reactions, a tt B obtains its Int by collision with the intasome, a n...
Ref 34Cited 109 Source Cite this paper
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