The Nucleosomal Surface as a Docking Station for Kaposi's Sarcoma Herpesvirus LANA-Reference-Cited by-同舟云学术

The Nucleosomal Surface as a Docking Station for Kaposi's Sarcoma Herpesvirus LANA

Published:2006-02-10 Issue:5762 Volume:311 Page:856-861
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Barbera Andrew J.¹²³⁴,Chodaparambil Jayanth V.¹²³⁴,Kelley-Clarke Brenna¹²³⁴,Joukov Vladimir¹²³⁴,Walter Johannes C.¹²³⁴,Luger Karolin¹²³⁴,Kaye Kenneth M.¹²³⁴

Affiliation:

1. Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.

2. Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523–1870, USA.

3. Department of Cancer Biology, Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA 02115, USA.

4. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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