Dual Functions of Largest NURF Subunit NURF301 in Nucleosome Sliding and Transcription Factor Interactions

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

doi:10.1016/s1097-2765(01)00345-8

Cited by 232 publications

(259 citation statements)

References 83 publications

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“…NURF also appears to have a role in X chromosome morphology [88] and steroid signaling during larval to pupal metamorphosis [89]. Transcriptional activation by NURF is brought about by mobilizing nucleosomes along the DNA [90] which requires the largest subunit of NURF, NURF 301 [91]. The direction of nucleosome mobilization is modulated by transcription factor Gal4 [92].…”

Section: Iswi Familymentioning

confidence: 99%

Mechanisms of ATP dependent chromatin remodeling

Gangaraju

Bartholomew

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

128

159

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The inter-relationship between DNA repair and ATP dependent chromatin remodeling has begun to become very apparent with recent discoveries. ATP dependent remodeling complexes mobilize nucleosomes along DNA, promote the exchange of histones, or completely displace nucleosomes from DNA. These remodeling complexes are often categorized based on the domain organization of their catalytic subunit. The biochemical properties and structural information of several of these remodeling complexes are reviewed. The different models for how these complexes are able to mobilize nucleosomes and alter nucleosome structure are presented incorporating several recent findings. Finally the role of histone tails and their respective modifications in ATP-dependent remodeling are discussed.

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Section: Iswi Familymentioning

confidence: 99%

Mechanisms of ATP dependent chromatin remodeling

Gangaraju

Bartholomew

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

128

159

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“…In the NURF complex, the NURF301 subunit modifies the intrinsic nucleosome mobilization properties of the ISWI polypeptide. (71) In addition, NURF301 was found to interact with sequence-specific transcription factors. (71) In the ACF and CHRAC complexes, the Acf1 subunit stimulates the intrinsic chromatin assembly and remodeling activities of ISWI.…”

Section: Activities Of Chromatin-remodeling Factorsmentioning

confidence: 99%

“…(71) In addition, NURF301 was found to interact with sequence-specific transcription factors. (71) In the ACF and CHRAC complexes, the Acf1 subunit stimulates the intrinsic chromatin assembly and remodeling activities of ISWI. (30,31,33,67,69) The Acf1 subunit also contains a DNA- binding region that is important for the chromatin assembly activity of ACF.…”

Section: Activities Of Chromatin-remodeling Factorsmentioning

confidence: 99%

“…(68,69) (2) Chromatin-remodeling factors can catalyze mobilization (which is sometimes termed 'sliding') of nucleosomes relative to the DNA template. (52,59,63,69,71,(77)(78)(79)(80)(81)(82)(83) (3) SNF2 subfamily complexes, but not ISWI subfamily complexes, can mediate the transfer of histones from one DNA template to a separate DNA template. (69,80,84,85) (4) SNF2 subfamily complexes catalyze the apparent disassembly of nucleosomes, as assessed by the loss of DNA supercoiling of chromatin templates.…”

Section: How Might Chromatin Remodeling Occur?mentioning

confidence: 99%

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Chromatin remodeling by ATP‐dependent molecular machines

2003

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SummaryThe eukaryotic genome is packaged into a periodic nucleoprotein structure termed chromatin. The repeating unit of chromatin, the nucleosome, consists of DNA that is wound nearly two times around an octamer of histone proteins. To facilitate DNA-directed processes in chromatin, it is often necessary to rearrange or to mobilize the nucleosomes. This remodeling of the nucleosomes is achieved by the action of chromatin-remodeling complexes, which are a family of ATP-dependent molecular machines. Chromatin-remodeling factors share a related ATPase subunit and participate in transcriptional regulation, DNA repair, homologous recombination and chromatin assembly. In this review, we provide an overview of chromatin-remodeling enzymes and discuss two possible mechanisms by which these factors might act to reorganize nucleosome structure.

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“…6 GAGA factor has been suggested to promote the formation of paused RNA Pol II by facilitating pre-initiation complex formation and the establishment of an open chromatin structure through the recruitment of components of the basal transcriptional machinery, such as TFIID, 6 and chromatin remodeling complexes, such as NURF and FACT. [30][31][32][33] Thus, GAF has been suggested to promote the recruitment of RNA Pol II that subsequently stalls.…”

Section: Sp3 Promotes Occupancy Of the Nelf Complexmentioning

confidence: 99%

Enforcing the pause: Transcription factor Sp3 limits productive elongation by RNA polymerase II

Valín

Gill²

2013

Cell Cycle

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Abbreviations: CDK, cyclin-dependent kinase; CTD, C-terminal domain of the RNA polymerase II; DSIF, DRB sensitivity-inducing factor; H3K4me3, histone H3 trimethylated at lysine 4; H3K36me3, histone H3 trimethylated at lysine 36; H3S10, histone H3 serine 10; NELF, negative elongation factor complex; P-TEFb, positive transcription elongation factor b; PP, protein phosphatase; p21 CIP1 , cyclin-dependent kinase inhibitor 1A; RNA Pol II, RNA polymerase II; SUMO, small ubiquitin-related modifier T he transition of paused RNA polymerase II into productive elongation is a highly dynamic process that serves to fine-tune gene expression in response to changing cellular environments. We have recently reported that the transcription factor Sp3 inhibits the transition of paused RNA Pol II to productive elongation at the promoter of the cyclin-dependent kinase inhibitor p21 CIP1 and other Sp3-repressed genes. Our studies support the view that Sp3 has three modes of action: activation, SUMO-Sp3-mediated heterochromatin silencing and SUMOindependent inhibition of elongation. At the p21 CIP1 promoter, binding of the positive elongation factor P-TEFb kinase was not affected by Sp3. In contrast, Sp3 promoted binding of the protein phosphatase PP1 to the p21 CIP1 promoter, suggesting that Sp3-dependent regulation of the local balance between kinase and phosphatase activities may contribute to gene expression. Our findings show that the transition of paused RNA Pol II to productive elongation is an important step regulated by both promoter-specific activators and repressors to finely modulate mRNA expression levels.

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Dual Functions of Largest NURF Subunit NURF301 in Nucleosome Sliding and Transcription Factor Interactions

Cited by 232 publications

References 83 publications

Mechanisms of ATP dependent chromatin remodeling

Mechanisms of ATP dependent chromatin remodeling

Chromatin remodeling by ATP‐dependent molecular machines

Enforcing the pause: Transcription factor Sp3 limits productive elongation by RNA polymerase II

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