BIOL 200 Lecture Notes - Lecture 3: Heterochromatin Protein 1, Chromodomain, Histone Code

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Lecture 3: chromatin dynamics and the histone code: chromatin dynamics. Nucleosome: middle part of histones interacts with other histones and forming the structure. For each histone there is a histone n- and c- terminal tail that sticks out. Amino-acids of that tail capable to interact with dna or proteins, very flexible. After a protein has been synthesized, there are enzyme that can modify amino acids of side chains (change chemical properties). Some amino acid side chains in histone tails are covalently modified post-translationally. Methylation of lysine or arginine amino group has 3 hydroxyl ions that can be replaced (mono, di- or trimethylation) Other modifications: small peptide (ubiquitin) can be added. Modifications can affect the charge on the histone and its electrostatic interactions with dna. Example: acetylation of lysine neutralizes its positive charge and reduces the interaction of histone with dna (cid:271)e(cid:272)o(cid:373)es the less (cid:862)(cid:271)eads o(cid:374) a st(cid:396)i(cid:374)g(cid:863) conformation conducive for transcription and replication.

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