作者: Tamara L. Caterino , Jeffrey J. Hayes
DOI: 10.1139/O10-024
关键词:
摘要: Linker histones are multifunctional proteins that involved in a myriad of processes ranging from stabilizing the folding and condensation chromatin to playing direct role regulating gene expression. However, how this class enigmatic binds accomplishes these functions remains unclear. Here we review data regarding H1 structure function chromatin, with special emphasis on C-terminal domain (CTD), which typically en- compasses approximately half mass linker histone includes large excess positively charged residues. Owing its amino acid composition, CTD was previously proposed as an unstructured poly- cation. structural studies have shown adopts detectable secondary when interacting DNA macromolecular crowding agents. We describe classic recent experiments defining do- main emerging indicating protein may be linked intrinsic disor- der.