Abstract
Transcription activation factors and multisubunit coactivator complexes get recruited at specific chromatin sites via protein domains that recognize histone modifications. Single PHDs (plant homeodomains) interact with differentially modified H3 histone tails. Double PHD finger (DPF) domains possess a unique structure different from PHD and are found in six proteins: histone acetyltransferases MOZ and MORF; chromatin remodeling complex BAF (DPF1–3); and chromatin remodeling complex PBAF (PHF10). Among them, PHF10 stands out due to the DPF sequence, structure, and functions. PHF10 is ubiquitously expressed in developing and adult organisms as four isoforms differing in structure (the presence or absence of DPF) and transcription regulation functions. Despite the importance of the DPF domain of PHF10 for transcription activation, its structure remains undetermined. We performed homology modeling of the human PHF10 DPF domain and determined common and distinct features in structure and histone modifications recognition capabilities, which can affect PBAF complex chromatin recruitment. We also traced the evolution of DPF1–3 and PHF10 genes from unicellular to vertebrate organisms. The data reviewed suggest that the DPF domain of PHF10 plays an important role in SWI/SNF-dependent chromatin remodeling during transcription activation.
Highlights
Gene expression is regulated by a variety of protein complexes
Double PHD finger (DPF) domains are present in six proteins, which actively participate in gene expression regulation
PHF10-P isoforms, as part of the PBAF complex, are recruited to promoter regions of neutrophil-specific surface receptor genes, which are expressed during differentiation
Summary
The chromatin epigenetic landscape, essential to the manifestation of genetic information, is shaped by histone modifications Both individual proteins and protein complex subunits capable of interacting with chromatin possess domains that recognize different modifications of N-terminal histone tails. DPF domains are present in six proteins, which actively participate in gene expression regulation. Two of these proteins, MOZ and MORF, are histone acetyltransferases, either of which can be part of the MYST complexes family acetylating H3 histone tails at lysines 9, 14, and. The SWI/SNF family includes PBAF, BAF, and ncBAF complexes consisting of many proteins These complexes possess identical cores and the ATPase subunit BRG1/BRM; their specific chromatin-binding modules differ. Mammalians have four PHF10 alternative splicing isoforms, which possess distinct domain structures and play different roles in gene transcription [17,18,19]
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