摘要Linker histones, e.g., H1, are best known for their ability to bind to nucleosomes and stabilize both nucleosome structure and condensed higher-order chromatin structures. However, over the years many investigators have report-ed specific interactions between linker histories and proteins involved in important cellular processes. The purpose of this review is to highlight evidence indicating an important alternative mode of action for HI, namely protein-protein interactions. We first review key aspects of the traditional view of linker histone action, including the importance of the HI C-terminal domain. We then discuss the current state of knowledge of linker historic interactions with other proteins, and, where possible, highlight the mechanism of linker histone-mediated protein-protein interactions. Taken together, the data suggest a combinatorial role for the linker histones, functioning both as primary chromatin archi-tectural proteins and simultaneously as recruitment hubs for proteins involved in accessing and modifying the chro-matin fiber.