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Cryo-EM structure of the Smc5/6 holo-complex.

Stephen T Hallett1, Isabella Campbell Harry1, Pascale Schellenberger2

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|August 22, 2022
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The Smc5/6 complex structure reveals how accessory proteins bind the core SMC. Mutations affecting this interaction impair Smc5/6 chromatin association and yeast growth.

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Area of Science:

  • Structural Biology
  • Molecular and Cell Biology
  • Biochemistry

Background:

  • The Smc5/6 complex is crucial for DNA repair, replication stress response, and antiviral defense.
  • Understanding its structure is key to elucidating its diverse cellular functions.

Purpose of the Study:

  • To determine the high-resolution structure of the budding yeast Smc5/6 holo-complex.
  • To understand the interaction between the Smc5/6 core and the Nse1/3/4 subcomplex.
  • To investigate the functional consequences of disrupting Smc5/6 interactions.

Main Methods:

  • Reconstitution of the Smc5/6 holo-complex from recombinant proteins.
  • Cryogenic electron microscopy (cryo-EM) for structural determination.
  • Site-directed mutagenesis and live-cell single molecule localization microscopy (SMLM).

Main Results:

  • The cryo-EM structure provides an architectural overview of the six-subunit Smc5/6 complex.
  • A specific loop in Smc5 (Smc5-loop) interacts with the Nse1 subunit.
  • Mutations in Nse1 affecting Smc5-loop binding cause slow growth and reduced chromatin association of Smc5/6.
  • Functional equivalence between KITE and HAWK accessory subunits was suggested.

Conclusions:

  • The Smc5/6 structure reveals critical interactions for complex assembly and function.
  • The Smc5-loop/Nse1 interaction is essential for Smc5/6 chromatin localization and cell viability.
  • Structural insights support functional parallels between different SMC complex accessory subunits.