ArticleJournal of bacteriology2006
Common and variable contributions of Fis residues to high-affinity binding at different DNA sequences.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Nucleoid-Associated Protein Fis Represses Type 3 Fimbriae to Modulate Biofilm and Adherence Formation inMicroorganisms · 2025Article
- Genome-wide promoter assembly inGenome research · 2022Article
- Facilitated dissociation of nucleoid-associated proteins from DNA in the bacterial confinement.Biophysical journal · 2022Article
- The Fis Nucleoid Protein Negatively Regulates the Phase VariationFrontiers in microbiology · 2022Article
- Crystal structure of the nucleoid-associated protein Fis (PA4853) from Pseudomonas aeruginosa.Acta crystallographica. Section F, Structural biology communications · 2020Article
- A bacteriophage mimic of the bacterial nucleoid-associated protein Fis.The Biochemical journal · 2020Article
- Cooperative DNA binding by proteins through DNA shape complementarity.Nucleic acids research · 2019Article
- Fis is a global regulator critical for modulation of virulence factor production and pathogenicity of Dickeya zeae.Scientific reports · 2018Article
- DNA Sequence Determinants Controlling Affinity, Stability and Shape of DNA Complexes Bound by the Nucleoid Protein Fis.PloS one · 2016Article
- Regulation of the vapBC-1 toxin-antitoxin locus in nontypeable Haemophilus influenzae.PloS one · 2012Article
- The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS.Protein science : a publication of the Protein Society · 2011Article
- Altered regulation of the OmpF porin by Fis in Escherichia coli during an evolution experiment and between B and K-12 strains.Journal of bacteriology · 2011Article
- The shape of the DNA minor groove directs binding by the DNA-bending protein Fis.Genes & development · 2010Article
- Biochemical identification of base and phosphate contacts between Fis and a high-affinity DNA binding site.Journal of molecular biology · 2008Article
- Functional characterization of the Escherichia coli Fis-DNA binding sequence.Journal of molecular biology · 2008Article
- Effect of random and hub gene disruptions on environmental and mutational robustness in Escherichia coli.BMC genomics · 2006Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Fis is a nucleoid-associated protein that interacts with poorly related DNA sequences with a high degree of specificity. A difference of more than 3 orders of magnitude in apparent Kd values was observed between specific (Kd, approximately 1 to 4 nM) and nonspecific (Kd, approximately 4 microM) DNA binding. To examine the contributions of Fis residues to the high-affinity binding at different DNA sequences, 13 alanine substitutions were generated in or near the Fis helix-turn-helix DNA binding motif, and the resulting proteins were purified. In vitro binding assays at three different Fis sites (fis P II, hin distal, and lambda attR) revealed that R85, T87, R89, K90, and K91 played major roles in high-affinity DNA binding and that R85, T87, and K90 were consistently vital for binding to all three sites. Other residues made variable contributions to binding, depending on the binding site. N84 was required only for binding to the lambda attR Fis site, and the role of R89 was dramatically altered by the lambda attR DNA flanking sequence. The effects of Fis mutations on fis P II or hin distal site binding in vitro generally correlated with their abilities to mediate fis P repression or DNA inversion in vivo, demonstrating that the in vitro DNA-binding effects are relevant in vivo. The results suggest that while Fis is able to recognize a minimal common set of DNA sequence determinants at different binding sites, it is also equipped with a number of residues that contribute to the binding strength, some of which play variable roles.
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