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Structure of the replication regulator Sap1 reveals functionally important interfaces.

Maria M Jørgensen1, Babatunde Ekundayo2, Mikel Zaratiegui3

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Summary
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The fission yeast protein Sap1 plays a key role in DNA replication fork stalling. Essential functions of Sap1 depend on its head-to-tail oligomerization, revealed through structural and mutation studies.

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Area of Science:

  • Molecular biology
  • Genetics
  • Structural biology

Background:

  • Programmed replication fork stalling is crucial for genome stability but its mechanisms are unclear.
  • The fission yeast protein Sap1 is involved in mating-type switching and programmed replication fork stalling.
  • Sap1 exhibits distinct DNA binding modes: head-to-head at the mating-type locus and head-to-tail at replication fork blocking sites.

Purpose of the Study:

  • To investigate the structural basis of Sap1's DNA binding and oligomerization.
  • To elucidate the role of Sap1 oligomerization in programmed replication fork stalling.

Main Methods:

  • Crystal structure determination of the Sap1 DNA binding domain.
  • Site-directed mutagenesis of Sap1 to analyze protein-DNA interactions and functional consequences.
  • Analysis of Sap1 mutations in the context of replication fork blockage.

Main Results:

  • The crystal structure revealed Sap1 molecules interacting in a head-to-tail arrangement compatible with DNA binding.
  • Mutations alleviating replication fork blockage at Tf2 transposons were mapped to the head-to-tail interface.
  • Lethal mutations were identified within this head-to-tail interface, indicating its essentiality.

Conclusions:

  • Sap1's essential functions, particularly in programmed replication fork stalling, rely on its head-to-tail oligomerization.
  • The head-to-tail oligomerization interface is critical for Sap1's biological activity and genome stability.