Communication Dans Un Congrès Année : 2021

The box c/d snornp assembly factor bcd1 interacts with the histone chaperone rtt106 and controls its transcription dependent activity

Résumé

Biogenesis of eukaryotic box C/D small nucleolar ribonucleoproteins initiates co-transcriptionally and requires the action of the assembly machinery including the Hsp90/R2TP complex, the Rsa1p:Hit1p heterodimer and the Bcd1 protein. We present genetic interactions between the Rsa1p-encoding gene and genes involved in chromatin organization including RTT106 that codes for the H3-H4 histone chaperone Rtt106p controlling H3K56ac deposition. We show that Bcd1p binds Rtt106p and controls its transcription-dependent recruitment by reducing its association with RNA polymerase II, modulating H3K56ac levels at gene body. We reveal the 3D structures of the free and Rtt106p-bound forms of Bcd1p using nuclear magnetic resonance and X-ray crystallography. The interaction is also studied by a combination of biophysical and proteomic techniques. Bcd1p interacts with a region that is distinct from the interaction interface between the histone chaperone and histone H3. Our results are evidence for a protein interaction interface for Rtt106p that controls its transcription-associated activity.

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Dates et versions

hal-03635843 , version 1 (08-04-2022)

Identifiants

  • HAL Id : hal-03635843 , version 1

Citer

Xavier Manival. The box c/d snornp assembly factor bcd1 interacts with the histone chaperone rtt106 and controls its transcription dependent activity. 2nd French congress on integrative structural biology, Nov 2021, Paris-Saclay, France. ⟨hal-03635843⟩
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