| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1946488 | Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms | 2013 | 12 Pages |
PICKLE plays a critical role in repression of genes that regulate development identity in Arabidopsis thaliana. PICKLE codes for a putative ATP-dependent chromatin remodeler that exhibits sequence similarity to members of subfamily II of animal CHD remodelers, which includes remodelers such as CHD3/Mi-2 that also restrict expression of developmental regulators. Whereas animal CHD3 remodelers are a component of the Mi-2/NuRD complex that promotes histone deacetylation, PICKLE promotes trimethylation of histone H3 lysine 27 suggesting that it acts via a distinct epigenetic pathway. Here, we examine whether PICKLE is also a member of a multisubunit complex and characterize the biochemical properties of recombinant PICKLE protein. Phylogenetic analysis indicates that PICKLE-related proteins in plants share a common ancestor with members of subfamily II of animal CHD remodelers. Biochemical characterization of PICKLE in planta, however, reveals that PICKLE primarily exists as a monomer. Recombinant PICKLE protein is an ATPase that is stimulated by ssDNA and mononucleosomes and binds to both naked DNA and mononucleosomes. Furthermore, recombinant PICKLE exhibits ATP-dependent chromatin remodeling activity. These studies demonstrate that subfamily II CHD proteins in plants, such as PICKLE, retain ATP-dependent chromatin remodeling activity but act through a mechanism that does not involve the ubiquitous Mi-2/NuRD complex.
► PICKLE-related proteins share a common ancestor with CHD3 chromatin remodelers. ► Homology modeling predicts that PICKLE has a SANT-SLIDE DNA-binding domain. ► Unlike animal CHD3 proteins, PICKLE primarily exists as a monomer. ► Recombinant PICKLE is an ATPase that is stimulated by ssDNA and mononucleosomes. ► Recombinant PICKLE exhibits ATP‐dependent chromatin remodeling activity.
