The Nucleosome Assembly Activity of NAP1 Is Enhanced by Alien

Eckey, Maren; Wang, Hong; Papaioannou, Maria; Baniahmad, Aria

doi:10.1128/mcb.01106-06

Cited by 32 publications

(24 citation statements)

References 44 publications

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“…24). To examine this, we measured the levels of histone deposition via a standard supercoiling assay24,35. Vps75, in the presence or absence of equimolar amounts of Rtt109, was incubated with Topoisomerase I-relaxed pUC19 plasmid and histones H3 and H4 under single-turnover conditions ([Vps75] or [Rtt109-Vps75] > [histones]).…”

Section: Resultsmentioning

confidence: 99%

Molecular functions of the histone acetyltransferase chaperone complex Rtt109–Vps75

Berndsen

Tsubota

Lindner

et al. 2008

Nat Struct Mol Biol

108

152

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Histone acetylation and nucleosome remodeling regulate DNA damage repair, replication and transcription. Rtt109, a recently discovered histone acetyltransferase (HAT) from Saccharomyces cerevisiae, functions with the histone chaperone Asf1 to acetylate lysine K56 on histone H3 (H3K56), a modification associated with newly synthesized histones. In vitro analysis of Rtt109 revealed that Vps75, a Nap1 family histone chaperone, could also stimulate Rtt109-dependent acetylation of H3K56. However, the molecular function of the Rtt109-Vps75 complex remains elusive. Here we have probed the molecular functions of Vps75 and the Rtt109-Vps75 complex through biochemical, structural and genetic means. We find that Vps75 stimulates the kcat of histone acetylation by ∼100-fold relative to Rtt109 alone and enhances acetylation of K9 in the H3 histone tail. Consistent with the In vitro evidence, cells lacking Vps75 showed a substantial reduction (60%) in H3K9 acetylation during S phase. X-ray structural, biochemical and genetic analyses of Vps75 indicate a unique, structurally dynamic Nap1-like fold that suggests a potential mechanism of Vps75-dependent activation of Rtt109. Together, these data provide evidence for a multifunctional HAT-chaperone complex that acetylates histone H3 and deposits H3-H4 onto DNA, linking histone modification and nucleosome assembly.

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Section: Resultsmentioning

confidence: 99%

Molecular functions of the histone acetyltransferase chaperone complex Rtt109–Vps75

Berndsen

Tsubota

Lindner

et al. 2008

Nat Struct Mol Biol

108

152

View full text Add to dashboard Cite

show abstract

“…The probes were incubated with 0.2 μg of purified GST, GST-CTCF, or GST-CTCF ZF. Recombinant proteins were prepared as described previously [70]. The binding reaction was performed in PBS ([pH 7.4], supplemented with 5 mM MgCl 2 , 1 mM ZnCl 2 , 1 mM DTT, 0.1% NP-40, and 10% Glycerol) for 15 min at room temperature in the presence of 200 ng/μl pdIdC.…”

Section: Methodsmentioning

confidence: 99%

CTCF Genomic Binding Sites in Drosophila and the Organisation of the Bithorax Complex

et al. 2007

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Insulator or enhancer-blocking elements are proposed to play an important role in the regulation of transcription by preventing inappropriate enhancer/promoter interaction. The zinc-finger protein CTCF is well studied in vertebrates as an enhancer blocking factor, but Drosophila CTCF has only been characterised recently. To date only one endogenous binding location for CTCF has been identified in the Drosophila genome, the Fab-8 insulator in the Abdominal-B locus in the Bithorax complex (BX-C). We carried out chromatin immunopurification coupled with genomic microarray analysis to identify CTCF binding sites within representative regions of the Drosophila genome, including the 3-Mb Adh region, the BX-C, and the Antennapedia complex. Location of in vivo CTCF binding within these regions enabled us to construct a robust CTCF binding-site consensus sequence. CTCF binding sites identified in the BX-C map precisely to the known insulator elements Mcp, Fab-6, and Fab-8. Other CTCF binding sites correlate with boundaries of regulatory domains allowing us to locate three additional presumptive insulator elements; “Fab-2,” “Fab-3,” and “Fab-4.” With the exception of Fab-7, our data indicate that CTCF is directly associated with all known or predicted insulators in the BX-C, suggesting that the functioning of these insulators involves a common CTCF-dependent mechanism. Comparison of the locations of the CTCF sites with characterised Polycomb target sites and histone modification provides support for the domain model of BX-C regulation.

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“…ChIP and re-ChIP were performed as previously described [19]. For ChIP in transfected COS-7 cells, 10% of the precleared supernatant was taken out as input.…”

Section: Chip and Re-chipmentioning

confidence: 99%

Bag‐1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors

Wang

Baniahmad

et al. 2009

FEBS Letters

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a b s t r a c tThe Bcl-2 associated athanogene 1M (Bag-1M) is known to repress the transactivation of the glucocorticoid receptor (GR). We report here that Bag-1M inhibits the action of GR via recruitment of corepressors, including nuclear receptor corepressor (NcoR) and silencing mediator for retinoic acid and thyroid hormone receptor (SMRT), and histone deacetylase (HDAC)3 to the genomic response element of a glucocorticoid-regulated human metallothionein IIa (hMTIIa) gene. A mutant GR lacking the interaction with BAG-1M fails to recruit the corepressors NcoR and SMRT. RNAi-mediated knock down of corepressors and the use of HDAC inhibitor relieved Bag-1M-induced repression on the transactivation of the GR. In addition, Bag-1M is not involved in the degradation of the receptor. These findings indicate a novel mechanism by which Bag-1M acts as a corepressor and downregulates the activity of the GR. Structured summary:

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The Nucleosome Assembly Activity of NAP1 Is Enhanced by Alien

Cited by 32 publications

References 44 publications

Molecular functions of the histone acetyltransferase chaperone complex Rtt109–Vps75

Molecular functions of the histone acetyltransferase chaperone complex Rtt109–Vps75

CTCF Genomic Binding Sites in Drosophila and the Organisation of the Bithorax Complex

Bag‐1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors

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