Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Single-Molecule Imaging Reveals the Mechanism Underlying Histone Loading of Schizosaccharomyces pombe AAA+ ATPase Abo1

  • Kang, Yujin (Department of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST)) ;
  • Cho, Carol (Department of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST)) ;
  • Lee, Kyung Suk (Department of Physics Education, Kongju National University) ;
  • Song, Ji-Joon (Department of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST)) ;
  • Lee, Ja Yil (Department of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST))
  • Received : 2020.12.07
  • Accepted : 2021.02.09
  • Published : 2021.02.28
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Abstract

Chromatin dynamics is essential for maintaining genomic integrity and regulating gene expression. Conserved bromodomain-containing AAA+ ATPases play important roles in nucleosome organization as histone chaperones. Recently, the high-resolution cryo-electron microscopy structures of Schizosaccharomyces pombe Abo1 revealed that it forms a hexameric ring and undergoes a conformational change upon ATP hydrolysis. In addition, single-molecule imaging demonstrated that Abo1 loads H3-H4 histones onto DNA in an ATP hydrolysis-dependent manner. However, the molecular mechanism by which Abo1 loads histones remains unknown. Here, we investigated the details concerning Abo1-mediated histone loading onto DNA and the Abo1-DNA interaction using single-molecule imaging techniques and biochemical assays. We show that Abo1 does not load H2A-H2B histones. Interestingly, Abo1 deposits multiple copies of H3-H4 histones as the DNA length increases and requires at least 80 bp DNA. Unexpectedly, Abo1 weakly binds DNA regardless of ATP, and neither histone nor DNA stimulates the ATP hydrolysis activity of Abo1. Based on our results, we propose an allosteric communication model in which the ATP hydrolysis of Abo1 changes the configuration of histones to facilitate their deposition onto DNA.

Keywords

Acknowledgement

This work was supported by the Samsung Science and Technology Foundation (SSTF-BA1901-13) to J.Y.L., the National Research Foundation (NRF-2020R1A2B5B01001792) to J.Y.L., (2020R1A2B5B03001517) to J.J.S., (2019R1A6A1A 10073887) to C.C., and (NRF-2019R1C1C1007124) to K.S.L.

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