Abstract
Our studies using proteases to probe protein structure establish that binding to the upstream activating sequences (UASs) of two different yeast a-specific genes induces a conformational change in the pheromone/receptor transcription factor (PRTF), which is not observed upon binding to the UASs of either of two alpha-specific genes. We propose that this selective structural alteration exposes an activation region of PRTF when it binds a-specific genes, switching these genes on. The transcriptional activator MAT alpha 1 may activate alpha-specific genes by binding to the PRTF-alpha-specific UAS complex and unmasking the otherwise hidden activation surface of PRTF. We also show that the N-terminal third of PRTF is sufficient for specific DNA binding, while the middle third of the protein interacts with MAT alpha 1.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Affinity Labels
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DNA / metabolism
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DNA-Binding Proteins / physiology*
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Fungal Proteins / ultrastructure*
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Gene Expression Regulation, Fungal
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Macromolecular Substances
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Mating Factor
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Peptide Fragments / metabolism
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Peptides / metabolism
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Protein Conformation
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Receptors, Cell Surface / physiology*
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Receptors, Mating Factor
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Receptors, Peptide*
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Regulatory Sequences, Nucleic Acid
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Saccharomyces cerevisiae / genetics*
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Structure-Activity Relationship
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Transcription Factors / physiology*
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Transcription, Genetic
Substances
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Affinity Labels
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DNA-Binding Proteins
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Fungal Proteins
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Macromolecular Substances
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Peptide Fragments
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Peptides
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Receptors, Cell Surface
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Receptors, Mating Factor
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Receptors, Peptide
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Transcription Factors
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Mating Factor
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DNA