Solution structure of the AT‐rich interaction domain of Jumonji/JARID2

Kusunoki, Hideki; Takeuchi, Takashi; Kohno, Toshiyuki

doi:10.1002/prot.22449

Cited by 9 publications

(12 citation statements)

References 28 publications

(7 reference statements)

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“…In view of this, it is perhaps surprising that the altered JmjC domain contained within Jarid2 is highly conserved (Figure 1d), a result that suggests that Jarid2 has a function that might be independent of histone demethylation. Although there are currently no biochemical data to support an alternative role for Jarid2, it has been claimed that its ARID and ZF domains directly bind DNA [8,34,35], albeit with low affinity [36]. In addition to these conserved domains, the N terminus of Jarid2 contains a nuclear localization sequence (Figure 1b) and a trans -repression domain that is required for repressor activity in Gal4 reporter systems [7,34].…”

Section: The Jumonji Family Of Histone Demethylasesmentioning

confidence: 99%

Inactive yet indispensable: the tale of Jarid2

Landeira

Fisher

2011

Trends in Cell Biology

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Methylation of histone tails is believed to be important for the establishment and inheritance of gene expression programs during development. Jarid2/Jumonji is the founding member of a family of chromatin modifiers with histone demethylase activity. Although Jarid2 contains amino acid substitutions that are thought to abolish its catalytic activity, it is essential for the development of multiple organs in mice. Recent studies have shown that Jarid2 is a component of the polycomb repressive complex 2 and is required for embryonic stem (ES) cell differentiation. Here, we discuss current literature on the function of Jarid2 and hypothesize that defects resulting from Jarid2 deficiency arise from a failure to correctly prime genes in ES cells that are required for later stages in development.

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Section: The Jumonji Family Of Histone Demethylasesmentioning

confidence: 99%

Inactive yet indispensable: the tale of Jarid2

Landeira

Fisher

2011

Trends in Cell Biology

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“…A solution structure of the Jarid2 ARID domain shows a structurally conserved core fold (helices H1 to H6) similar to those of other ARID domains with an additional helix H7 which forms a cruciform with helix H1. 34 Chemical shift perturbation studies with DNA oligonucleotides show small shifts except in N-and C-terminal residues of the domain. The residues of the DNA binding HTH motif show small shifts indicating that DNA binding occurs with low affinity.…”

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confidence: 99%

Composition, recruitment and regulation of the PRC2 complex

Nayak

Xu²,

Min³

2011

Nucleus

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T he PRC2 histone methyltransferase complex is an important regulator of gene expression programs in metazoans. Gene expression regulation by the PRC2 complex is critical for development and cell differentiation. Several recent studies have begun to shed light on the molecular basis for the physiological function of the PRC2 complex. Here, we discuss some of these results and how they provide new insights into the composition, recruitment and regulation of the PRC2 complex.

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“…S2,) 16. The presence of the additional helix at the C terminus suggests that yeast SWI1 ARID belongs to a C ‐terminal extended ARID domain 17–20. The solution structure of yeast SWI1 ARID was then determined by a set of NMR spectra.…”

Section: Resultsmentioning

confidence: 99%

“…However, the orientation of the additional C ‐terminal helix in yeast SWI1 ARID domain is opposite to that in mouse Jumonji/JARID2 ARID domain. The helix in the ARID domain of mouse Jumonji/JARID2 forms a cruciform with H1 (the first helix of the conserved region among the ARID family) while the helix stretches away from the H1 in the case of yeast SWI1 ARID domain 19. A short β‐hairpin is present in the structures of the ARID domains of DRI and mouse Jumonji/JARID2, while it is absent in the other ARID domains including yeast SWI ARID domain 19.…”

Section: Resultsmentioning

confidence: 99%

Solution structure of SWI1 AT‐rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA

Wang

Zhang

et al. 2012

Proteins

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SWI1 is a subunit of the SWI/SNF complex involved in chromatin remodeling. It contains an AT-rich interaction domain (ARID) which has the potential DNA binding activity. In this study, we determined the solution structure of the SWI1 ARID domain from Saccharomyces cerevisiae by nuclear magnetic resonance spectroscopy. Yeast SWI1 ARID domain is composed of seven alpha helices, six of which are conserved among the ARID family. In addition, the DNA-binding activity of the SWI1 ARID domain was confirmed by chemical shift perturbation assay. Similar to its human homolog, the yeast SWI1 ARID domain binds DNA nonspecifically.

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Solution structure of the AT‐rich interaction domain of Jumonji/JARID2

Cited by 9 publications

References 28 publications

Inactive yet indispensable: the tale of Jarid2

Inactive yet indispensable: the tale of Jarid2

Composition, recruitment and regulation of the PRC2 complex

Solution structure of SWI1 AT‐rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA

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