Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Histone tails undergo methylation at their lysines and arginines. These chemical marks act as traffic signals that direct activity of chromatin remodeling complexes to appropriate regions of the genome. A surprisingly diverse group of effector protein modules in chromatin remodeling complexes and their associated factors are involved in the recognition of histone methyllysines. Previous studies generally painted a picture of individual lysines recognized by these protein modules in a 1:1 fashion. However, recent structural studies show more complex interactions where the critical lysines are recognized in pairs, or in the context of nucleosomal DNA, or within the central pore of repeat motifs. These interactions extend our understanding of how histone tail recognition can be enhanced through coupled interactions within a single module or through the cooperation of two different molecules.

More information Original publication

DOI

10.1016/j.sbi.2011.10.001

Type

Journal article

Publication Date

2011-12-01T00:00:00+00:00

Volume

21

Pages

744 - 749

Total pages

5

Addresses

D, i, a, b, e, t, e, s, , a, n, d, , O, b, e, s, i, t, y, , R, e, s, e, a, r, c, h, , C, e, n, t, e, r, ,, , S, a, n, f, o, r, d, -, B, u, r, n, h, a, m, , M, e, d, i, c, a, l, , R, e, s, e, a, r, c, h, , I, n, s, t, i, t, u, t, e, ,, , 6, 4, 0, 0, , S, a, n, g, e, r, , R, o, a, d, ,, , O, r, l, a, n, d, o, ,, , F, L, , 3, 2, 8, 2, 7, ,, , U, S, A, ., , s, e, p, i, d, e, h, @, s, a, n, f, o, r, d, b, u, r, n, h, a, m, ., o, r, g

Keywords

Chromatin, Nucleosomes, Animals, Humans, Lysine, Histones, DNA, Protein Conformation, Methylation, Models, Molecular