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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Rad50 zinc hook functions as a constitutive dimerization module interchangeable with SMC hinge.

Hisashi Tatebe1, Chew Theng Lim1, Hiroki Konno2

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The Mre11/Rad50 complex, crucial for genome maintenance, opens at its head domains, similar to SMC proteins. Its Rad50 hook acts as a stable dimerization interface, conserved across species.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The Mre11/Rad50 complex is vital for maintaining genome stability.
  • Previous studies suggested transient opening at the Rad50 zinc hook.

Purpose of the Study:

  • To elucidate the structural dynamics and conserved functions of the Mre11/Rad50 complex.
  • To compare the Mre11/Rad50 complex architecture with SMC proteins.

Main Methods:

  • High-speed atomic force microscopy (HS-AFM) for nanoscale imaging.
  • Functional analysis of chimeric Mre11/Rad50 complexes in yeast.

Main Results:

  • HS-AFM revealed consistent bridging of Rad50 arms by dimerized hooks and head domain uncoupling during ring opening.
  • These structural features are conserved in yeast and bacteria.
  • A chimeric complex with a bacterial SMC hinge functionally replaced the Rad50 hook in DNA repair.

Conclusions:

  • The Mre11/Rad50 complex opens via head domain disconnection, analogous to SMC proteins.
  • The Rad50 hook functions as a stable dimerization interface, similar to an SMC hinge.