The Nucleosomal Surface as a Docking Station for Kaposi's Sarcoma Herpesvirus LANA
- 10 February 2006
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 311 (5762), 856-861
- https://doi.org/10.1126/science.1120541
Abstract
Kaposi's sarcoma–associated herpesvirus (KSHV) latency-associated nuclear antigen (LANA) mediates viral genome attachment to mitotic chromosomes. We find that N-terminal LANA docks onto chromosomes by binding nucleosomes through the folded region of histones H2A-H2B. The same LANA residues were required for both H2A-H2B binding and chromosome association. Further, LANA did not bind Xenopus sperm chromatin, which is deficient in H2A-H2B; chromatin binding was rescued after assembly of nucleosomes containing H2A-H2B. We also describe the 2.9-angstrom crystal structure of a nucleosome complexed with the first 23 LANA amino acids. The LANA peptide forms a hairpin that interacts exclusively with an acidic H2A-H2B region that is implicated in the formation of higher order chromatin structure. Our findings present a paradigm for how nucleosomes may serve as binding platforms for viral and cellular proteins and reveal a previously unknown mechanism for KSHV latency.This publication has 37 references indexed in Scilit:
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