Daxx is a ubiquitously expressed protein that functions, in part, as a transcriptional co-repressor through its interaction with a growing numberof nuclear, DNA-associated proteins. Human Daxx contains four structural domains commonly found in transcriptional regulatory proteins: two predicted paired amphipathic helices, an acid-rich domain and a Ser/Pro/Thr (SPT)-rich domain. The post-translational modification status of the SPT-domain of hDaxx regulates its association with transcription factors such as Pax3 and ETS-1, effectively bringing hDaxx to sites of active transcription.Through its presence at the site of active transcription, hDaxx could then be able to associate with acetylated histones present in the nucleosomes andDek that is associated with chromatin. Through its association with the SPT-domain of hDaxx, histone deacetylases may also be brought to the site of active transcription. As a consequence, nucleosomes in the vicinity of the site of active transcription will have the histone tails deacetylated, allowing the deactylated tail to bind to DNA, thereby leading to an inactive chromatin structure and transcriptional repression []. The Daxx protein (also known as the Fas-binding protein or death domain-associated protein 6) is thought to play a role in apoptosis as a component of nuclear promyelocytic leukemia protein (PML) oncogenic domains (PODS). Daxx associates with PODs through a direct interaction withPML, a critical component of PODs. The interaction is a dynamic, cell cycle regulated event and is dependent on the post-translational modification of PML by the small ubiquitin-related modifier SUMO-1.
The Daxx protein (also known as death domain-associated protein 6) is thought to play a role in apoptosis. Daxx forms a complex with Axin []. Daxx is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C [].
The Daxx protein (also known as death domain-associated protein 6) is thought to play a role in apoptosis. Daxx forms a complex with Axin []. Daxx is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C [].
Daxx (also known as death domain-associated protein 6) is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. Daxx is also a histone chaperone conserved in metazoa that acts specifically on histone H3.3. This entry represents the histone-binding domain of Daxx that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer [, , , , , ].
Daxx (also known as death domain-associated protein 6) is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. Daxx is also a histone chaperone conserved in metazoa that acts specifically on histone H3.3. This entry represents the histone-binding domain of Daxx that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer [, , , , , ].
Microspherule protein 1 (MCRS1 or MSP58) is an RNA-binding protein that interacts with Daxx transcriptional regulator, relieving its repressor activity. Overexpression of MCRS1 leads to translocation of Daxx to the enlarged nucleoli in COS-1 or 293 cells []. It also interacts with fragile X messenger ribonucleoprotein 1 (FMRP), which represses specific mRNAs being transported as silent ribonucleoparticles from the cell body of a neuron to the distant synapse. MCRS1 binds to the G-quadruplex structures of the mRNA []. MCRS1 is a component of the NSL complex [], the MLL1/MLL complex [], and is a putative regulatory component in the chromatin remodeling INO80 complex []. The isoform MCRS2 is a cell-cycle-dependent protein which accumulates in the early S phase, and interacts with the telomerase-inhibitory protein LPTS/PinX1 [].
This is a family of major tegument proteins from Herpesviruses. Herpesvirus tegument proteins counteract the intrinsic anti-viral defenses and support the early steps of infection. BNRF1 is the Epstein-Barr virus (EBV) major tegument protein and plays an important role in viral transport from the endosomes to the nucleus []. Furthermore, it supports EBV early infection by interacting with host nuclear protein Daxx and disrupting the formation of the Daxx-ATRX chromatin remodeling complex [].
