Sandbox Aryan 20221057 BI3323-Aug2025

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(== Summary == PDB **8YNY** (4.52 Å cryo-EM) captures Cas9-sgRNA post-cleavage binding to nucleosome linker DNA (PAM1).[web:2] <Jmol width=100% height=500px>load =8YNY; cartoon on; color chain; spin y)

Revision as of 18:31, 30 November 2025

Contents

Structure Overview

Cas9-sgRNA ribonucleoprotein targets nucleosome **linker DNA** (PAM1/PAM28) and **entry-exit regions** (SHL6), avoiding tightly wrapped **core DNA** (SHL0-5). Native-PAGE on Widom 601 nucleosomes confirmed preferential cleavage at DNA ends where transient unwrapping occurs.[attached_file:1]

The post-cleavage complex shows HNH/REC2 domains disordered, bridge helix absent, and target/non-target DNA strands cleaved—consistent with binary biochemical data.[web:2]

PI Domain Interactions

Cas9's **PI domain** (residues ~1100-1368) makes multiple contacts: - **Histone tails**: Weak electrostatic interaction (non-essential for binding) - **PI edge (K1155)**: Lysine stabilizes post-cleavage complex via DNA phosphate backbone - **Core DNA loops (H1264/R1298/K1300)**: Nonspecific binding inhibits cleavage

    • Mutagenesis validation**: H1264A/R1298Q/K1300A mutants increase nucleosome binding AND cleavage efficiency both in vitro and rice callus genome editing.[attached_file:1]

Dual Inhibition Mechanism

1. **Access barrier**: Nucleosome DNA ends inflexible (SHL0-5), blocking Cas9 binding 2. **Motion restriction**: PI-core DNA trapping limits HNH/RuvC domain movements for cleavage

    • Entry/exit asymmetry** from Widom601 sequence flexibility explains variable editing across chromatin contexts.[web:14]

Implications

Reveals Cas9's eukaryotic adaptation strategy and identifies **chromatin-optimized variants** for improved genome editing tools.[web:121]

Scene 1: Ternary complex - DNA unwrapping
Scene 1: Ternary complex - DNA unwrapping
Scene 2: PI domain contacts (red residues)
Scene 2: PI domain contacts (red residues)
Scene 3: Mutant sites (orange spheres)
Scene 3: Mutant sites (orange spheres)

BI3323-Aug2025

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