Roles and activities of chromatin remodeling ATPases in plants

Abstract

These authors contributed equally to this paper. SUMMARYChromatin remodeling ATPases and their associated complexes can alter the accessibility of the genome in the context of chromatin by using energy derived from the hydrolysis of ATP to change the positioning, occupancy and composition of nucleosomes. In animals and plants, these remodelers have been implicated in diverse processes ranging from stem cell maintenance and differentiation to developmental phase transitions and stress responses. Detailed investigation of their roles in individual processes has suggested a higher level of selectivity of chromatin remodeling ATPase activity than previously anticipated, and diverse mechanisms have been uncovered that can contribute to the selectivity. This review summarizes recent advances in understanding the roles and activities of chromatin remodeling ATPases in plants.

Lineage-specific stem cells, signals and asymmetries during stomatal development

“…Emerging evidence has revealed that epigenetic, chromatin-based regulation, including DNA methylation, histone modification, nucleosome remodeling and regulation by non-coding RNAs, plays a central role in self-renewal, differentiation and reprogramming in both the animal and plant kingdoms (Fisher and Fisher, 2011;Han et al, 2015;Ikeuchi et al, 2015;Orkin and Hochedlinger, 2011). A number of epigenetic regulators have been implicated in the myogenic lineage program.…”

Fundamental and applied research in ABA signaling: Regulation by ABA of the chromatin remodeling ATPase BRAHMA and biotechnological use of the PP2CA promoter.

“…It has the canonical domains found in this family of proteins (Farrona et al, 2004, Han et al, 2015. BRM protein includes a N-terminal region with a glutamine-rich domain and a helicase SANT-associated domain (HSA).…”

“…The SnAC domain is known to be required for mobilizing nucleosomes and its presence is required in vivo for transcription regulation but not for the complex organization, the substrate recognition or the recruitment function (Sen et al, 2013, Sen et al, 2011. BRM has a C-terminal domain that contains an AT-hook and a bromodomain (Farrona et al, 2007, Sen et al, 2011, Han et al, 2015. The AT-hook and the bromodomain are important domains for the BRM association with chromatin.…”

“…BRM is an SWI/SNF subgroup ATPase and has the canonical domains found in this family of proteins (Han et al, 2015) ( Figure 20). BRM has an N-terminal region with a glutamine-rich domain and a helicase SANT-associated domain (HSA), which frequently serves as docking site for recruiting transcription factors such as leafy (LFY) and TCP family transcription factor 4 (TCP4) (Farrona et al, 2004, Szerlong et al, 2008, Efroni et al, 2013.…”

“…BRM has an N-terminal region with a glutamine-rich domain and a helicase SANT-associated domain (HSA), which frequently serves as docking site for recruiting transcription factors such as leafy (LFY) and TCP family transcription factor 4 (TCP4) (Farrona et al, 2004, Szerlong et al, 2008, Efroni et al, 2013. This is followed by the catalytic helicase-like ATPase domain, the Snf2 ATP-coupling (SnAC) domain, and a C-terminal domain which contains an AT-hook and a bromodomain; these domains are important for catalytic activity of BRM and for BRM association with chromatin, respectively (Farrona et al, 2007, Sen et al, 2011, Han et al, 2015. We confirmed and extended this interaction by BiFC assays in tobacco epidermal cells, and showed that SnRK2.2, SnRK2.3 and SnRK2.6 kinases were able to interact with BRMN and BRMC ( Figure 23A).…”