Abstract
In an effort to understand the structure function relationship of TFIIH, a transcription/repair factor, we focused our attention on the p44 subunit, which plays a central role in both mechanisms. The amino-terminal portion of p44 has been shown to be involved in the regulation of the XPD helicase activity; here we show that its carboxyl-terminal domain is essential for TFIIH transcription activity and that it binds three zinc atoms through two independent modules. The first contains a C4 zinc finger motif, whereas the second is characterized by a CX(2)CX(2-4)FCADCD motif, corresponding to interleaved zinc binding sites. The solution structure of this second module reveals an unexpected homology with the regulatory domain of protein kinase C and provides a framework to study its role at the molecular level.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cysteine* / genetics
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Cysteine* / metabolism
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DNA Helicases / chemistry
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DNA Helicases / genetics
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DNA Helicases / metabolism
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Histidine / genetics
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Histidine / metabolism
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Humans
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Mass Spectrometry
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Nuclear Magnetic Resonance, Biomolecular
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Protein Binding
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Protein Kinase C / chemistry
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Structure-Activity Relationship
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Transcription Factor TFIIH
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription Factors, TFII*
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Transcription, Genetic
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Zinc / metabolism
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Zinc Fingers*
Substances
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Protein Subunits
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Recombinant Proteins
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Transcription Factors
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Transcription Factors, TFII
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Transcription Factor TFIIH
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Histidine
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Protein Kinase C
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DNA Helicases
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Zinc
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Cysteine