Abstract
Polycomb group (PcG) and Trithorax group (TrxG) proteins are evolutionarily conserved factors responsible for the repression and activation of the transcription of multiple genes in Drosophila and mammals. Disruption of the PcG/TrxG expression is associated with many pathological conditions, including cancer, which makes them suitable targets for diagnosis and therapy in medicine. In this review, we focus on the major PcG and TrxG complexes, the mechanisms of PcG/TrxG action, and their recruitment to chromatin. We discuss the alterations associated with the dysfunction of a number of factors of these groups in oncology and the current strategies used to develop drugs based on small-molecule inhibitors.
Highlights
Establishment and maintenance of precise gene expression patterns that are unique to each cell type is required for the proper functioning of multicellular organisms
Tremendous progress has been made in the study of how the Polycomb group (PcG)/Trithorax group (TrxG) system functions
The increasing complexity of the PcG/TrxG system in the process of evolution from invertebrates to mammals and the emergence of numerous paralogs of these proteins represent a challenge for researchers: to what extent the currently understood composition of protein complexes is characteristic of all types of cells? Are they unique only to a number of tissues and/or developmental stages and do they differ in others? Numerous recent studies assign a crucial role to the spatial organization of genes in the nucleus
Summary
Establishment and maintenance of precise gene expression patterns that are unique to each cell type is required for the proper functioning of multicellular organisms. Five proteins – Osa, Brm, Mor, Snr1, and SAYP – which behave as TrxG factors in genetic tests in Drosophila, were shown to be subunits of the SWI/SNF subfamily of the ATP-dependent chromatin remodeler complexes: BAP (Brahma-associated proteins) and PBAP (Polybromo-associated BAP) [80,81,82,83]. The dCBP, Trx, and Trr proteins, as well as the modifications H3K4me1 and H3K27Ac catalyzed by them, respectively, were shown to colocalize at active enhancers and at the regions of PcG proteins recruitment in Drosophila.
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