Histone Modifications

2023

Full text Open access: Gold Metadata (CSL-JSON)
DOI 10.1007/978-3-031-27133-5_7
Data confidence 70 medium
How this score is calculated

It is built from checkable properties of the record itself: whether the article has a DOI, how many independent sources confirmed its data, whether the required fields are filled in, and how recent the latest confirmation is. Disagreement between sources and a missing identifier lower it. A value of 80 or above means the record was published without further checking; 60 to 79 means it is published at reduced confidence, with a manual check advisable. A record verified by an editor by hand is never pushed below 90 by a recalculation. This scores our data about the article, not the article itself.

Abstract

In this chapter, we will present posttranslational modifications as a general mechanism for instructing proteins about their function. Moreover, they allow proteins to “memorize” their encounters, such as contacts with other proteins. Histone proteins are the key examples of this protein communication system. In particular, lysine acetylations and methylations of histone tails have a large functional impact. Genome-wide profiling of the large set of posttranscriptional histone modifications provides the basis of the histone code. This code leads to the understanding, how the epigenome directs transcriptional regulation and stores information. Histone modifying enzymes, such as HATs, HDACs, KMT and lysine demethylases (KDMs), either add or remove posttranslational modifications to histone proteins and in this way change the functional profile of the epigenome.