Inorganic pyrophosphatase is a component of the Drosophila nucleosome remodeling factor complex

Article Abstract:

Inorganic pyrophosphatase is one part of the nucleosome remodeling factor (NURF) complex of Drosophila. NURF of Drosophila is a protein complex made up of four polypeptides. In vitro the complex is helpful to perturbation of chromatin structure in an ATP-dependent way. The smallest, 38-kD, component of NURF has been characterized and cloned. Recombinant NURF-38 by itself and the pure NURF complex have inorganic pyrophosphatase activity. NURF-38 is very noticably homologous to inorganic pyrophosphatases that are known.

Phosphatases, Pyrophosphates

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ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF

Article Abstract:

A study was conducted to investigate the remodelng action of Drosophila's nucleosome remodeling factor (NURF) on an adenosine triphosphate-dependent histone octamer complexed with DNA. Results suggest that the NURF is capable of putting the histone octamer in vicinal positions on the same DNA fragment while maintaining the full complement of core histones. It was also observed that remodeling the NURF results in the reduction of activation energy for short-range sliding of a histone octamer.

Histones, Chromatin

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The Drosophila nucleosome remodeling factor NURF is required for Ecdysteroid signaling and metamorphosis

Article Abstract:

2540The whole genome expression analysis was performed on mutants lacking the nucleosome remodeling factor (NURF)-specific subunit NURF301 to determine in vivo gene targets of 'Drosophila' NURF. It is found that Null mutants do not undergo larval to pupal metamorphosis and also enhance dominant-negative mutations in ecdysone receptor moreover, purified NURF binds EcR in an ecdysone-dependent manner suggesting it is a direct effector of nuclear receptor activity.

United States, Science & research, Research, Ecdysteroids, Nucleosomes

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