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Human DNA polymerase α in binary complex with a DNA:DNA template-primer.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • The Polα/primase complex is crucial for DNA replication initiation in eukaryotes, synthesizing RNA-DNA primers.
  • Understanding how the polymerase subunit interacts with different DNA substrates is key to explaining replication termination.

Purpose of the Study:

  • To determine the structural basis for primer termination during eukaryotic DNA replication.
  • To elucidate the interaction of the human Polα polymerase subunit with a DNA:DNA helix.

Main Methods:

  • X-ray crystallography was used to obtain the structure of the human Polα polymerase subunit.
  • The structure was analyzed in complex with a DNA:DNA helix.

Main Results:

  • The first crystal structure of human Polα polymerase subunit complexed with a DNA:DNA helix is presented.
  • The DNA:DNA helix interacting with the polymerase adopts an unexpected hybrid A-B form, deviating from the canonical B-form.
  • Key polymerase-primer contacts observed with RNA primers are conserved with DNA primers.

Conclusions:

  • Primer termination by Polα polymerase may result from the energetic cost of distorting the DNA:DNA helix from B-form to a hybrid A-B form.
  • This structural distortion, rather than a loss of specific molecular contacts, is proposed as the mechanism for eukaryotic primer synthesis termination.