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Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli.
Fis is a small basic DNA-binding protein from Escherichia coli that was identified because of its role in site-specific DNA recombination reactions. Recent evidence indicates that Fis alsoExpand
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Isolation of spontaneously derived mutants of Caulobacter crescentus.
Caulobacter crescentus has a penicillinase which precludes the use of penicillin for mutant enrichment. However, two other antibiotics, fosfomycin and D-cycloserine, can be enrich for C. crescentusExpand
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Sequence, regulation, and functions of fis in Salmonella typhimurium.
The fis operon from Salmonella typhimurium has been cloned and sequenced, and the properties of Fis-deficient and Fis-constitutive strains were examined. The overall fis operon organization in S.Expand
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The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures.
The mammalian high mobility group proteins HMG1 and HMG2 are abundant, chromatin-associated proteins whose cellular function is not known. In this study we show that these proteins can substitute forExpand
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The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding.
NHP6A is a non-sequence-specific DNA-binding protein from Saccharomyces cerevisiae which belongs to the HMGB protein family. Previously, we have solved the structure of NHP6A in the absence of DNAExpand
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Variable structures of Fis-DNA complexes determined by flanking DNA-protein contacts.
The Fis protein from Escherichia coli and Salmonella typhimurium regulates many diverse reactions including recombination, transcription, and replication and is one of the most abundant DNA bindingExpand
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Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions.
The structure of the 52-amino acid DNA-binding domain of the prokaryotic Hin recombinase, complexed with a DNA recombination half-site, has been solved by x-ray crystallography at 2.3 angstromExpand
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Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non‐sequence‐specific binding
NHP6A is a chromatin‐associated protein from Saccharomyces cerevisiae belonging to the HMG1/2 family of non‐specific DNA binding proteins. NHP6A has only one HMG DNA binding domain and formsExpand
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Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA
The multistep kinetics through which DNA-binding proteins bind their targets are heavily studied, but relatively little attention has been paid to proteins leaving the double helix. Using single-DNAExpand
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Mechanism of chromosome compaction and looping by the Escherichia coli nucleoid protein Fis.
Fis, the most abundant DNA-binding protein in Escherichia coli during rapid growth, has been suspected to play an important role in defining nucleoid structure. Using bulk-phase and single-DNAExpand
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