Abstract
NURF is an ISWI complex of four proteins that uses the energy of ATP hydrolysis to catalyze nucleosome sliding. Three NURF components have been identified previously. We have cloned cDNA encoding the largest NURF subunit, revealing a 301 kDa polypeptide (NURF301) that shares structural motifs with ACF1. We have reconstituted full and partial NURF complexes from recombinant proteins and show that NURF301 and the ISWI ATPase are necessary and sufficient for accurate and efficient nucleosome sliding. An HMGA/HMGI(Y)-like domain of NURF301 that facilitates nucleosome sliding indicates the importance of DNA conformational changes in the sliding mechanism. NURF301 also shows interactions with sequence-specific transcription factors, providing a basis for targeted recruitment of the NURF complex to specific genes.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Chromosomal Proteins, Non-Histone*
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Cloning, Molecular
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Drosophila Proteins*
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Drosophila melanogaster / physiology
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Humans
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Insect Proteins / chemistry
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Insect Proteins / genetics
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Insect Proteins / metabolism*
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Macromolecular Substances
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Molecular Sequence Data
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nucleosomes / genetics
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Nucleosomes / metabolism*
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Protein Structure, Tertiary
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Alignment
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Transcription Factors / metabolism*
Substances
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Chromosomal Proteins, Non-Histone
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Drosophila Proteins
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E(bx) protein, Drosophila
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Insect Proteins
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Macromolecular Substances
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Nuclear Proteins
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Nucleosomes
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Recombinant Proteins
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Transcription Factors