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- W2026778867 abstract "•The intrinsically disordered protein nature of MeCP2 is critical for its manifold interactions and functions. •MeCP2 is an extremely abundant chromosomal protein in neurons. •In addition to Rett syndrome, MeCP2 is involved in other neurological disorders. •MeCP2 activity is regulated by many post-translational modifications (PTMs). Since the discovery of its fundamental involvement in Rett syndrome, methyl CpG binding protein 2 (MeCP2) has been the focus of an exhaustive biochemical and functional characterization. It is now becoming apparent that the intrinsic highly disordered nature of MeCP2, which is amenable to a plethora of post-translational modifications (PTMs), allows it to recognize a large number of protein interacting partners, including histones. MeCP2 is highly abundant in the brain and it is an important component of neuronal chromatin; nevertheless, the organization and implications of its involvement in terms of DNA methylation binding dependence and effects on transcription are still not well understood. Recent results have shown that MeCP2 plays an important role in brain development, aging, and in neurological disorders. Since the discovery of its fundamental involvement in Rett syndrome, methyl CpG binding protein 2 (MeCP2) has been the focus of an exhaustive biochemical and functional characterization. It is now becoming apparent that the intrinsic highly disordered nature of MeCP2, which is amenable to a plethora of post-translational modifications (PTMs), allows it to recognize a large number of protein interacting partners, including histones. MeCP2 is highly abundant in the brain and it is an important component of neuronal chromatin; nevertheless, the organization and implications of its involvement in terms of DNA methylation binding dependence and effects on transcription are still not well understood. Recent results have shown that MeCP2 plays an important role in brain development, aging, and in neurological disorders. a group of neurodevelopmental disorders characterized by deficits in social and communicative interaction and stereotypic behaviors. a nucleoprotein complex formed by the interaction of histones and other chromosomal proteins with genomic DNA in eukaryotes. the average distance in nucleotides between two adjacent nucleosomes for the chromatin of a given tissue. small (100–130 amino acid) histones consisting of an intrinsically disordered N-terminal domain (tail) and a structurally organized dimerizing C-terminal ‘histone fold’ domain. Two H2A–H2B dimers are associated with a H3–H4 tetramer forming the protein ‘core’ of the nucleosome. one of the most abundant chromosomal protein components of chromatin. These are basic proteins which are rich in arginine and lysine amino acids. a group of proteins that do not exhibit any secondary or tertiary structure in a solution but that can acquire such organization upon interaction with other protein partners or nucleic acids. lysine-rich proteins (∼30% lysine) of approximately 200 amino acids. They consist of a central globular winged helix domain (WHD) flanked by N- and C- terminal disordered domains. They bind to the DNA at the entry and exit sites of the nucleosome and to the linker DNA regions of the chromatin fiber. a member of the methyl-binding domain (MBD) family of proteins that binds to methylated symmetrical 5′ CpG pairs. disease resulting from a progressive partial or complete loss of neuronal function. disease arising from alterations of the brain and central nervous system that occur during development and result in an impairment of the proper growth and function of these organs. the fundamental repeating subunit of chromatin consisting of approximately 146 DNA bp wrapped about the histone core in 1.75 left-handed superhelical turns. Nucleosome core particles are connected within the chromatin fiber by a variable length DNA region (∼20–70 bp) known as ‘linker DNA’. modifications of proteins that take place after their synthesis in the ribosome. They usually involve the covalent attachment of biochemically functional groups (acetyl, methyl, phosphate, etc.) or other proteins (i.e., ubiquitin) to specific amino acids. The reactions are carried out by highly specialized enzymes such as acetyl/methyl transferases, kinases, or ubiquitin ligases. These modifications carry important functional and/or structural implications. protein regions, consisting of at least 12 amino acids in length, that are highly enriched in proline (P), glutamic (E), serine (S), and threonine (T) residues. It is hypothesized that they typically signal (to the proteins containing them) for rapid proteolytic degradation by the 26S ubiquitin proteasome system (UPS). a multimeric adenosine triphosphate (ATP)-dependent protein complex (26S proteasome) that catalyzes the degradation of multiubiquitinated proteins." @default.
- W2026778867 created "2016-06-24" @default.
- W2026778867 creator A5001104135 @default.
- W2026778867 creator A5010137759 @default.
- W2026778867 creator A5021832837 @default.
- W2026778867 date "2014-09-01" @default.
- W2026778867 modified "2023-10-13" @default.
- W2026778867 title "MeCP2: the long trip from a chromatin protein to neurological disorders" @default.
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