Dual functions of largest NURF subunit NURF301 in nucleosome sliding and transcription factor interactions

Hua Xiao, Raphael Sandaltzopoulos, Hih Min Wang, Ali Hamiche, Ryan Ranallo, Kyu Min Lee, Dragony Fu, Carl Wu

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165 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)531-543
Number of pages13
JournalMolecular Cell
Volume8
Issue number3
DOIs
Publication statusPublished - 2001
Externally publishedYes

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ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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