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| Title | Structural Basis for HIV-1 Rev Recognition by the Histone Chaperone Human Nap1. |
|---|---|
| Journal, issue, pages | J Biol Chem, Page 113120, Year 2026 |
| Publish date | May 6, 2026 |
Authors | Elif Eren / Norman R Watts / Dennis C Winkler / Paul T Wingfield / ![]() |
| PubMed Abstract | Human Nap1 (hNap1) is a histone chaperone involved in chromatin dynamics and has been shown to interact with the HIV-1 regulatory protein Rev, which is essential for nuclear export of viral RNA. ...Human Nap1 (hNap1) is a histone chaperone involved in chromatin dynamics and has been shown to interact with the HIV-1 regulatory protein Rev, which is essential for nuclear export of viral RNA. Despite the functional significance of this interaction, its structural basis has remained elusive. Here, we present the X-ray crystal structure of hNap1 and the cryo-electron microscopy structure of the core domain of hNap1-Rev complex. The structure reveals that hNap1 binds Rev dimers via its acidic concave surface, engaging the Rev arginine-rich motif and oligomerization domain, and stabilizes Rev as a dimer-of-dimers tetramer. This interaction prevents higher-order Rev aggregation and enhances Rev's cooperative binding to the Rev Response Element. Surface plasmon resonance measurements confirm the formation of a stable complex with an apparent low-micromolar affinity between hNap1 and Rev, supporting a chaperone-like, reversible association. Our findings provide molecular insight into how hNap1 modulates Rev assembly and function, suggesting a model in which hNap1 primes Rev for productive engagement with viral RNA, thereby facilitating HIV-1 replication. |
External links | J Biol Chem / PubMed:42103228 |
| Methods | EM (single particle) / X-ray diffraction / EM (helical sym.) |
| Resolution | 3.2 - 8.3 Å |
| Structure data | EMDB-75601, PDB-11bc: ![]() PDB-11bd: ![]() PDB-11be: |
| Source |
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Keywords | CHAPERONE / histone chaperone / H2A-H2B / Nap1 / HIV-1 Rev / Nucleosome assembly protein 1 / Nucleosome assembly protein like 1 / Histone / VIRAL PROTEIN / HIV-1 / Rev / Filament / Rev Response Element / RNA / RNA binding protein |
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homo sapiens (human)
human immunodeficiency virus 1
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