4.8 Article

Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing

Journal

NUCLEIC ACIDS RESEARCH
Volume 45, Issue 7, Pages 3888-3905

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/nar/gkx081

Keywords

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Funding

  1. National Research Foundation of Korea (NRF) - Korea government [MEST] [2015R1A2A1A0 5001694, NRF-2013M3A6A4044580]
  2. Rising Star Program (POSTECH)
  3. BK21 Program (Ministry of Education)
  4. Public Health Service Awards [R01 GM066094, R01 GM090063]
  5. NIGMS/National Institutes of Health
  6. NRF [Korean Ministry of Science and Education] [2015R1A2A1A05001694]
  7. National Research Foundation of Korea [2015R1A2A1A05001694] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Regulatory inactivation of DnaA (RIDA) is one of the major regulatory mechanisms of prokaryotic replication licensing. In RIDA, the Hda-sliding clamp complex loaded onto DNA directly interacts with adenosine triphosphate (ATP)-bound DnaA and stimulates the hydrolysis of ATP to inactivate DnaA. A prediction is that the activity of Hda is tightly controlled to ensure that replication initiation occurs only once per cell cycle. Here, we determined the crystal structure of the Hda-beta clamp complex. This complex contains two pairs of Hda dimers sandwiched between two beta clamp rings to form an octamer that is stabilized by three discrete interfaces. Two separate surfaces of Hda make contact with the beta clamp, which is essential for Hda function in RIDA. The third interface between Hda monomers occludes the active site arginine finger, blocking its access to DnaA. Taken together, our structural and mutational analyses of the Hda-beta clamp complex indicate that the interaction of the beta clamp with Hda controls the ability of Hda to interact with DnaA. In the octameric Hda-beta clamp complex, the inability of Hda to interact with DnaA is a novel mechanism that may regulate Hda function.

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