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XB-ART-722
Science February 10, 2006; 311 (5762): 856-61.

The nucleosomal surface as a docking station for Kaposi''s sarcoma herpesvirus LANA.

Barbera AJ , Chodaparambil JV , Kelley-Clarke B , Joukov V , Walter JC , Luger K , Kaye KM .


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.

PubMed ID: 16469929
Article link: Science
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: h2ac21 h2bc21