Degradation of S. cerevisiae Cohesin with the Auxin-Inducible Degron System

Brocas, Clémentine; Ducrot, Cécile; Dubrana, Karine

doi:10.1007/978-1-4939-9520-2_2

Cited by 3 publications

(1 citation statement)

References 16 publications

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“…To investigate the role of cohesin in DSB end-tethering, we employed the auxin-induced degron (AID) system to deplete the cohesin subunit Smc1 ( 29 ). Following a 1-hour auxin incubation, Smc1 protein levels were substantially reduced and maintained at near undetectable levels for over 4 hours (fig.…”

Section: Resultsmentioning

confidence: 99%

Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks

Phipps,

Toulouze,

Ducrot

et al. 2023

Preprint

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DNA double-strand breaks (DSB) must be repaired to ensure genome stability. Crucially, DSB ends must be kept together for timely repair. InSaccharomyces cerevisiae, two poorly understood pathways mediate DSB end-tethering. One employs the Mre11-Rad50-Xrs2 (MRX) complex to physically bridge DSB ends. Another requires the conversion of DSB ends into single-strand DNA (ssDNA) by Exo1, but the bridging proteins are unknown. We uncover that cohesin, its loader and Smc5/6 act with Exo1 to tether DSB ends. Remarkably, cohesin specifically impaired in oligomerization fails to tether DSB ends, revealing a new function for cohesin oligomerization. In addition to the known importance of sister chromatid cohesion, microscopy-based microfluidic experiments unveil a new role for cohesin in repair by ensuring DSB end-tethering. Altogether, our findings demonstrate that oligomerization of cohesin prevents DSB end separation and promotes DSB repair, revealing a novel mode of action and role for cohesin in safeguarding genome integrity.

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Section: Resultsmentioning

confidence: 99%

Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks

Phipps,

Toulouze,

Ducrot

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

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Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks

Phipps,

Toulouze,

Ducrot

et al. 2024

Nat Cell Biol

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Rapid depletion of target proteins in plants by an inducible protein degradation system

Huang,

Rojas-Pierce

2024

The Plant Cell

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Inducible protein knockdowns are excellent tools to test the function of essential proteins in short time scales and to capture the role of proteins in dynamic events. Current approaches destroy or sequester proteins by exploiting plant biological mechanisms such as the activity of photoreceptors for optogenetics or auxin-mediated ubiquitination in auxin degrons. It follows that these are not applicable for plants as light and auxin are strong signals for plant cells. We describe here an inducible protein degradation system in plants named E3-DART for E3-targeted Degradation of Plant Proteins. The E3-DART system is based on the specific and well-characterized interaction between the Salmonella secreted protein H1 (SspH1) and its human target protein kinase N1 (PKN1). This system harnesses the E3 catalytic activity of SspH1 and the SspH1-binding activity of the Homology Region 1b (HR1b) domain from PKN1. Using Nicotiana benthamiana and Arabidopsis (Arabidopsis thaliana), we show that a chimeric protein containing the Leucine-Rich Repeat (LRR) and novel E3 ligase (NEL) domains of SspH1 efficiently targets protein fusions of varying sizes containing HR1b for degradation. Target protein degradation was induced by transcriptional control of the chimeric E3 ligase using a glucocorticoid transactivation system and target protein depletion was detected as early as 3 h after induction. This system could be used to study the loss of any plant protein with high temporal resolution and may become an important tool in plant cell biology.

show abstract

Degradation of S. cerevisiae Cohesin with the Auxin-Inducible Degron System

Cited by 3 publications

References 16 publications

Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks

Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks

Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks

Rapid depletion of target proteins in plants by an inducible protein degradation system

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