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Structures and operating principles of the replisome

  1. Author:
    Gao, Yang
    Cui, Yanxiang
    Fox,Tara
    Lin, Shiqiang
    Wang, Huaibin
    De Val Alda,Natalia
    Zhou, Z. Hong
    Yang, Wei
  2. Author Address

    NIDDK, Lab Mol Biol, NIH, Bethesda, MD 20892 USA.Univ Calif Los Angeles, Calif NanoSyst Inst, Los Angeles, CA 90095 USA.NCI, Ctr Mol Microscopy, Ctr Canc Res, NIH, Bethesda, MD 20892 USA.Leidos Biomed Res Inc, Frederick Natl Lab Canc Res, Canc Res Technol Program, Frederick, MD 21701 USA.Fujian Agr & Forestry Univ, Coll Life Sci, Fuzhou, Fujian, Peoples R China.
    1. Year: 2019
    2. Date: Feb 22
    3. Epub Date: 2019 01 24
  1. Journal: Science (New York, N.Y.)
  2. AMER ASSOC ADVANCEMENT SCIENCE,
    1. 363
    2. Pages: 835-+
  3. Type of Article: Article
  4. Article Number: eaav7003
  5. ISSN: 0036-8075
  1. Abstract:

    Visualization in atomic detail of the replisome that performs concerted leading- and lagging-DNA strand synthesis at a replication fork has not been reported. Using bacteriophage T7 as a model system, we determined cryo-electron microscopy structures up to 3.2-angstroms resolution of helicase translocating along DNA and of helicase-polymerase-primase complexes engaging in synthesis of both DNA strands. Each domain of the spiral-shaped hexameric helicase translocates sequentially hand-over-hand along a single-stranded DNA coil, akin to the way AAA+ ATPases (adenosine triphosphatases) unfold peptides. Two lagging-strand polymerases are attached to the primase, ready for Okazaki fragment synthesis in tandem. A beta hairpin from the leading-strand polymerase separates two parental DNA strands into a T-shaped fork, thus enabling the closely coupled helicase to advance perpendicular to the downstream DNA duplex. These structures reveal the molecular organization and operating principles of a replisome.

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External Sources

  1. DOI: 10.1126/science.aav7003
  2. PMID: 30679383
  3. WOS: 000459387100034

Library Notes

  1. Fiscal Year: FY2018-2019
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