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The results suggest that ATRX (show ATRX Proteins) is required to limit replication stress during cellular proliferation, whereas upregulation of PARP-1 (show PARP1 Proteins) activity functions as a compensatory mechanism to protect stalled forks, limiting genomic damage, and facilitating late-born neuron production.
Our study highlights the importance of the cooperation between Rad54 and Mus81 (show MUS81 Proteins) for mediating DNA DSB repair and restraining chromosome missegregation.
The long noncoding RNA, TERRA (show DMRT2 Proteins) can bind both in cis (show CISH Proteins) to telomeres and in trans to genic targets; a large network of interacting proteins was defined, including epigenetic factors, telomeric proteins, and the RNA helicase, ATRX (show ATRX Proteins). TERRA (show DMRT2 Proteins) and ATRX (show ATRX Proteins) share hundreds of target genes and are functionally antagonistic at these loci: whereas TERRA (show DMRT2 Proteins) activates, ATRX (show ATRX Proteins) represses gene expression.
The changes of ATRX (show ATRX Proteins) distribution occur and partially correlate with the main stages of zygotic genome activation during mouse early development, butthese changes seem to be determined by other processes of structural and functional rearrangements of blastomere nuclei.
ATRX (show ATRX Proteins) mutation is associated with increased mutation rate at the single-nucleotide variant (SNV) level.
Daxx (show DAXX Proteins) and Atrx (show ATRX Proteins) safeguard the genome by silencing repetitive elements when DNA methylation (show HELLS Proteins) levels are low.
A direct role of Atrx (show ATRX Proteins) in the establishment and robust maintenance of heterochromatin is demonstrated.
We propose a model whereby ATRX-dependent deposition of H3.3 into heterochromatin is normally required to maintain the memory of silencing at imprinted loci.
ATRX (show ATRX Proteins) promotes the incorporation of histone H3.3 (show H3F3A Proteins) at particular transcribed genes and facilitates transcriptional elongation through G-rich sequences.
Using X chromosome inactivation as a model, study applied an unbiased proteomics approach to isolate Xist and PRC2 regulators and identified ATRX (show ATRX Proteins); ATRX (show ATRX Proteins) functions as a high-affinity RNA-binding protein that directly interacts with RepA/Xist RNA to promote loading of PRC2 in vivo. Without ATRX (show ATRX Proteins), PRC2 cannot load onto Xist RNA nor spread in cis (show CISH Proteins) along the X chromosome.
Nap1 (show IL8 Proteins) binds to RAD54 (show ATRX Proteins).
TAF12 (show TAF12 Proteins) and NFYC (show NFYC Proteins) are transcription factors that regulate the epigenome, whereas RAD54L (show ATRX Proteins) plays a central role in DNA repair
support a model in which RAD54L (show ATRX Proteins) and RAD54B (show RAD54B Proteins) counteract genome-destabilizing effects of direct binding of RAD51 (show RAD51 Proteins) to dsDNA in tumor cells
The RAD54L (show ATRX Proteins) polymorphism (2290C/T) can be used as a genetic marker inside the consensus deletion region at 1p32 in human meningiomas.
Shortened telomeres in murine scid (show PRKDC Proteins) cells expressing mutant RAD54L (show ATRX Proteins) coincide wirth reduction in recombination at telomeres.
hRad54, a Swi2/Snf2 (show SMARCA2 Proteins) protein, binds HJ-like structures with high specificity and promotes their bidirectional branch migration in an ATPase-dependent manner
Some immortal cells use the alternative lengthening of telomeres (ALT) pathway to maintain their telomeres instead of telomerase. This is the first genetic evidence that Rad54 is dispensable for the ALT pathway.
RAD54 (show ATRX Proteins) is recruited by RAD51 (show RAD51 Proteins)-ssDNA filament to the chromatin of the intact chromosome and it remodels that chromatin to facilitate accessibility for strand exchange
analysis of human rad54 (show ATRX Proteins) protein interactions with branched DNA molecules
Rad54 (show ATRX Proteins) protein causes dissociation of joint molecules by ATP-dependent branch-migration and therefore plays an important role in double strand DNA break repair.
Rad54 structure suggests that SWI2/SNF2 (show SMARCA4 Proteins) proteins use a mechanism analogous to helicases to translocate on dsDNA
The protein encoded by this gene belongs to the DEAD-like helicase superfamily, and shares similarity with Saccharomyces cerevisiae Rad54, a protein known to be involved in the homologous recombination and repair of DNA. This protein has been shown to play a role in homologous recombination related repair of DNA double-strand breaks. The binding of this protein to double-strand DNA induces a DNA topological change, which is thought to facilitate homologous DNA paring, and stimulate DNA recombination. Alternative splicing results in multiple transcript variants encoding the same protein.
, RAD54-like protein
, RAD54-like (S. cerevisiae)
, ATP-dependent helicase ATRX
, HP1 alpha-interacting protein
, X-linked nuclear protein
, alpha thalassemia/mental retardation syndrome (X-linked)
, heterochromatin protein 2
, transcriptional regulator ATRX
, DNA repair and recombination protein RAD54-like
, RAD54 homolog
, putative recombination factor GdRad54