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Review
. 2023 Apr 1;37(7-8):259-260.
doi: 10.1101/gad.350627.123. Epub 2023 Apr 12.

Chromosome organization by fine-tuning an ATPase

Lucia F Massari  1 , Adele L Marston  2
Affiliations
Review

Chromosome organization by fine-tuning an ATPase

Lucia F Massari et al. Genes Dev. .

Abstract

Cohesin is an ATPase that drives chromosome organization through the generation of intramolecular loops and sister chromatid cohesion. Cohesin's ATPase is stimulated by Scc2 binding but attenuated by acetylation of its Smc3 subunit. In this issue of Genes & Development, Boardman and colleagues (pp. 277-290) take a genetic approach to generate a mechanistic model for the opposing regulation of cohesin's ATPase by Scc2 and Smc3 acetylation. Their findings provide in vivo insight into how this important genome organizer functions in vivo.

Keywords: ATPase; ECO1; ESCO1; NIPBL; SCC2; SMC; acetylation; cohesin; cohesion.

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Figures

Figure 1.
Figure 1.
Smc3 acetylation opposes Scc2-dependent stimulation of cohesin's ATPase. Cycles of Scc2-stimulated ATP hydrolysis drive cohesin loading and loop extrusion. Smc3 acetylation blocks loading and loop extrusion, thereby anchoring loops and stabilizing cohesion. Boardman et al. (2023) provide genetic evidence that Scc2 modulates ATPase activity through interactions with Smc1 and that these interactions are blocked by Smc3 acetylation. Note that Scc3 is not shown for simplicity.
See this image and copyright information in PMC

References

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