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Structural Insight into BLM Recognition by TopBP1.

Luxin Sun1, Yuhao Huang1, Ross A Edwards1

  • 1Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada.

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|September 19, 2017
PubMed
Summary
This summary is machine-generated.

Topoisomerase IIβ binding protein 1 (TopBP1) binds Bloom syndrome helicase (BLM) at phospho-Ser304, not phospho-Ser338. This interaction, revealed by crystal structure, is crucial for genome stability and DNA replication checkpoint control.

Keywords:
BLMBRCTBloom syndromeTopBP1X-ray crystallographyfluorescence polarizationphosphopeptide interactions

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Area of Science:

  • Molecular biology
  • Genetics
  • Biochemistry

Background:

  • Topoisomerase IIβ binding protein 1 (TopBP1) is a key protein in DNA replication checkpoint control.
  • TopBP1's BRCT5 domain was hypothesized to interact with Bloom syndrome helicase (BLM) to maintain genome stability.

Purpose of the Study:

  • To elucidate the specific interaction between TopBP1 BRCT5 and BLM.
  • To determine the structural basis for TopBP1-BLM interaction in genome stability regulation.

Main Methods:

  • X-ray crystallography to determine the structure of TopBP1 BRCT4/5 bound to BLM.
  • Biochemical assays to analyze binding affinities and interaction interfaces.

Main Results:

  • TopBP1 BRCT5 specifically recognizes the BLM region around phospho-Ser304 (pSer304), not phospho-Ser338 (pSer338).
  • Crystal structure reveals TopBP1's pSer-binding pocket recognizes pSer304, and an N-terminal FVPP motif interacts with a hydrophobic groove on BRCT5.
  • The binding interface on BRCT5 is shared with MDC1 but with reversed binding orientations; BLM interaction shows higher affinity due to electrostatics and hydrophobicity.

Conclusions:

  • The interaction between TopBP1 and BLM is mediated by pSer304 and an adjacent FVPP motif, contributing to genome stability.
  • The binding mechanism highlights conserved evolutionary interactions, potentially involving TopBP1 and 53BP1.