ArticleProtein science : a publication of the Protein Society2000
Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Mutations to transcription factor MAX allosterically increase DNA selectivity by altering folding and binding pathways.Nature communications · 2025Article
- Basic helix-loop-helix pioneer factors interact with the histone octamer to invade nucleosomes and generate nucleosome-depleted regions.Molecular cell · 2023Article
- Genome recognition by MYC.Cold Spring Harbor perspectives in medicine · 2014Review
- Crystal structure of the minimalist Max-E47 protein chimera.PloS one · 2012Article
- Spectral analysis of sequence variability in basic-helix-loop-helix (bHLH) protein domains.Evolutionary bioinformatics online · 2007Article
- DNA bending by bHLH charge variants.Nucleic acids research · 2006Article
- Assembly of b/HLH/z proteins c-Myc, Max, and Mad1 with cognate DNA: importance of protein-protein and protein-DNA interactions.Biochemistry · 2005Article
- Regulation of phosphate acquisition in Saccharomyces cerevisiae.Current genetics · 2003Review
- Characterization of binding-induced changes in dynamics suggests a model for sequence-nonspecific binding of ssDNA by replication protein A.Protein science : a publication of the Protein Society · 2002Article
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Authors and funding
3 authors.
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Abstract
Backbone dynamics of the basic/helix-loop-helix domain of Pho4 from Saccharomyces cerevisae have been probed by NMR techniques, in the absence of DNA, nonspecifically bound to DNA and bound to cognate DNA. Alpha proton chemical shift indices and nuclear Overhauser effect patterns were used to elucidate the secondary structure in these states. These secondary structures are compared to the co-crystal complex of Pho4 bound to a cognate DNA sequence (Shimizu T. Toumoto A, Ihara K, Shimizu M, Kyogou Y, Ogawa N, Oshima Y, Hakoshima T, 1997, EMBO J 15: 4689-4697). The dynamic information provides insight into the nature of this DNA binding domain as it progresses from free in solution to a specifically bound DNA complex. Relative to the unbound form, we show that formation of either the nonspecific and cognate DNA bound complexes involves a large change in conformation and backbone dynamics of the basic region. The nonspecific and cognate complexes, however, have nearly identical secondary structure and backbone dynamics. We also present evidence for conformational flexibility at a highly conserved glutamate basic region residue. These results are discussed in relation to the mechanism of sequence specific recognition and binding.
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