title: Revisiting the structure and functions of the linker histone C-terminal tail domain.
abstract: Linker histones stabilize folded chromatin, acting through their long C-terminal tails. The C-termini contain high percentages of evenly distributed lysine and arginine residues and have no secondary structure in solution. Hence, it has generally been believed that the C-termini function by shielding negative charges on the DNA backbone. However, recent evidence supports a mechanism of action of the linker histone C-terminus that involves formation of specific secondary structure(s) upon interaction with other components of the chromatin fiber.
authors.affiliation: Department of Biochemistry, The University of Texas Health Science Center at San Antonio, 78229, USA.
authors.forename: Xu
authors.initials: X
authors.lastname: Lu
authors.forename: Jeffrey C
authors.initials: JC
authors.lastname: Hansen
mesh_terms: D000818:Animals; D002843:Chromatin / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D013329:Structure-Activity Relationship
chemical_list: D002843:Chromatin; D006657:Histones; D004247:DNA