On Friday November 24, 2017 around 5 pm EST portions of Xenbase may be intermittently available.

Click on this message to dismiss it.
Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
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 .

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: CA82036 NCI NIH HHS , GM067777 NIGMS NIH HHS , GM62267 NIGMS NIH HHS , R01 GM067777-05 NIGMS NIH HHS , R01 GM067777 NIGMS NIH HHS

Genes referenced: hist2h2ab hist2h2be

My Xenbase: [ Log-in / Register ]
version: [4.6.0]

Major funding for Xenbase is provided by the National Institute of Child Health and Human Development, grant P41 HD064556