Abstract
In spite of the large amount of sequence conservation among the DNA binding segments of basic region leucine zipper (bZIP) proteins, these proteins can discriminate differently between target sequences that differ in half-site spacing. Here it is shown that the half-site spacing preferences of bZIP proteins are the result of (i) the differential intrinsic curvature in target binding sites that differ by insertion or deletion of a single base pair and (ii) the ability of some bZIP proteins to overcome this intrinsic curvature through a mechanism dependent on basic segment residues.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Activating Transcription Factor 2
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Amino Acid Sequence
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Base Sequence
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Basic-Leucine Zipper Transcription Factors
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Binding Sites
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Cyclic AMP Response Element-Binding Protein / chemistry
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Cyclic AMP Response Element-Binding Protein / metabolism*
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DNA / chemistry
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DNA / metabolism*
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism*
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism*
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G-Box Binding Factors
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Leucine Zippers*
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Molecular Sequence Data
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Nucleic Acid Conformation
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Oligodeoxyribonucleotides / chemistry
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Oligodeoxyribonucleotides / metabolism
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Protein Kinases / chemistry
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Protein Kinases / metabolism*
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Proto-Oncogene Proteins c-jun / chemistry
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Proto-Oncogene Proteins c-jun / metabolism
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Saccharomyces cerevisiae Proteins*
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Transcription Factors*
Substances
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Activating Transcription Factor 2
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Basic-Leucine Zipper Transcription Factors
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Cyclic AMP Response Element-Binding Protein
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DNA-Binding Proteins
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Fungal Proteins
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G-Box Binding Factors
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Oligodeoxyribonucleotides
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Proto-Oncogene Proteins c-jun
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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DNA
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Protein Kinases