Unknown

Dataset Information

0

Molecular basis for DPY-30 association to COMPASS-like and NURF complexes.


ABSTRACT: DPY-30 is a subunit of mammalian COMPASS-like complexes (complex of proteins associated with Set1) and regulates global histone H3 Lys-4 trimethylation. Here we report structural evidence showing that the incorporation of DPY-30 into COMPASS-like complexes is mediated by several hydrophobic interactions between an amphipathic ? helix located on the C terminus of COMPASS subunit ASH2L and the inner surface of the DPY-30 dimerization/docking (D/D) module. Mutations impairing the interaction between ASH2L and DPY-30 result in a loss of histone H3K4me3 at the ? locus control region and cause a delay in erythroid cell terminal differentiation. Using overlay assays, we defined a consensus sequence for DPY-30 binding proteins and found that DPY-30 interacts with BAP18, a subunit of the nucleosome remodeling factor complex. Overall, our results indicate that the ASH2L/DPY-30 complex is important for cell differentiation and provide insights into the ability of DPY-30 to associate with functionally divergent multisubunit complexes.

SUBMITTER: Tremblay V 

PROVIDER: S-EPMC5832440 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Molecular basis for DPY-30 association to COMPASS-like and NURF complexes.

Tremblay Véronique V   Zhang Pamela P   Chaturvedi Chandra-Prakash CP   Thornton Janet J   Brunzelle Joseph S JS   Skiniotis Georgios G   Shilatifard Ali A   Brand Marjorie M   Couture Jean-François JF  

Structure (London, England : 1993) 20141120 12


DPY-30 is a subunit of mammalian COMPASS-like complexes (complex of proteins associated with Set1) and regulates global histone H3 Lys-4 trimethylation. Here we report structural evidence showing that the incorporation of DPY-30 into COMPASS-like complexes is mediated by several hydrophobic interactions between an amphipathic α helix located on the C terminus of COMPASS subunit ASH2L and the inner surface of the DPY-30 dimerization/docking (D/D) module. Mutations impairing the interaction betwee  ...[more]

Similar Datasets

| S-EPMC3457544 | biostudies-literature
| S-EPMC4690523 | biostudies-literature
| S-EPMC3152501 | biostudies-literature
2013-08-31 | GSE48413 | GEO
| S-EPMC3572774 | biostudies-literature
| S-EPMC3187824 | biostudies-literature
| S-EPMC6319814 | biostudies-literature
| S-EPMC6948180 | biostudies-literature
| S-EPMC7039682 | biostudies-literature
2013-08-31 | E-GEOD-48413 | biostudies-arrayexpress