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Hector Teece 2026-06-19 10:04:12 -04:00
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These tails are topic to several publish-translational covalent modifications, together with acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been found on a range of lysine residues in varied histones: K4 (using the single-letter amino-acid code for lysine), K9, K27, K36 and K79 in histone H3, K20 in histone H4, K59 within the globular area of histone H4 2 and K26 of histone H1B three A number of proteins answerable for the methylation of particular residues have been characterised, and all but certainly one of these comprises a SET area; they make up the SET-area protein methyltransferase household (Desk 1 ). The exception to the rule is the DOT1 household, members of which methylate K79 in the globular area of histone H3 and which are structurally not related to SET-domain proteins 4 - 6 Recent work means that SET-domain-containing proteins methylate a number of proteins in addition to histones (see later); they need to subsequently be named protein lysine methyltransferases somewhat than histone lysine methyltransferases.
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