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The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η

Author

Listed:
  • Chikahide Masutani

    (Institute for Molecular and Cellular Biology, Osaka University)

  • Rika Kusumoto

    (Institute for Molecular and Cellular Biology, Osaka University
    Nara Institute of Science and Technology (NAIST))

  • Ayumi Yamada

    (Institute for Molecular and Cellular Biology, Osaka University
    Graduate School of Pharmaceutical Science, Osaka University)

  • Naoshi Dohmae

    (Institute of Physical and Chemical Research (RIKEN))

  • Masayuki Yokoi

    (Institute for Molecular and Cellular Biology, Osaka University
    Institute of Physical and Chemical Research (RIKEN))

  • Mayumi Yuasa

    (Institute for Molecular and Cellular Biology, Osaka University)

  • Marito Araki

    (Institute for Molecular and Cellular Biology, Osaka University
    Graduate School of Pharmaceutical Science, Osaka University
    Institute of Physical and Chemical Research (RIKEN))

  • Shigenori Iwai

    (Biomolecular Engineering Research Institute)

  • Koji Takio

    (Institute of Physical and Chemical Research (RIKEN))

  • Fumio Hanaoka

    (Institute for Molecular and Cellular Biology, Osaka University
    Institute of Physical and Chemical Research (RIKEN))

Abstract

Xeroderma pigmentosum variant (XP-V) is an inherited disorder which is associated with increased incidence of sunlight-induced skin cancers. Unlike other xeroderma pigmentosum cells (belonging to groups XP-A to XP-G), XP-V cells carry out normal nucleotide-excision repair processes but are defective in their replication of ultraviolet-damaged DNA1,2. It has been suspected for some time that the XPV gene encodes a protein that is involved in trans-lesion DNA synthesis, but the gene product has never been isolated. Using an improved cell-free assay for trans-lesion DNA synthesis, we have recently isolated a DNA polymerase from HeLa cells that continues replication on damaged DNA by bypassing ultraviolet-induced thymine dimers in XP-V cell extracts3. Here we show that this polymerase is a human homologue of the yeast Rad30 protein, recently identified as DNA polymerase η (ref. 4). This polymerase and yeast Rad30 are members of a family of damage-bypass replication proteins5,6,7,8,9,10 which comprises the Escherichia coli proteins UmuC and DinB and the yeast Rev1 protein. We found that all XP-V cells examined carry mutations in their DNA polymerase η gene. Recombinant human DNA polymerase η corrects the inability of XP-V cell extracts to carry out DNA replication by bypassing thymine dimers on damaged DNA. Together, these results indicate that DNA polymerase η could be the XPV gene product.

Suggested Citation

  • Chikahide Masutani & Rika Kusumoto & Ayumi Yamada & Naoshi Dohmae & Masayuki Yokoi & Mayumi Yuasa & Marito Araki & Shigenori Iwai & Koji Takio & Fumio Hanaoka, 1999. "The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η," Nature, Nature, vol. 399(6737), pages 700-704, June.
    • Handle: RePEc:nat:nature:v:399:y:1999:i:6737:d:10.1038_21447
    DOI: 10.1038/21447
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    Cited by:

    1. Caleb Chang & Christie Lee Luo & Yang Gao, 2022. "In crystallo observation of three metal ion promoted DNA polymerase misincorporation," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Brittany N. Vandenberg & Marian F. Laughery & Cameron Cordero & Dalton Plummer & Debra Mitchell & Jordan Kreyenhagen & Fatimah Albaqshi & Alexander J. Brown & Piotr A. Mieczkowski & John J. Wyrick & S, 2023. "Contributions of replicative and translesion DNA polymerases to mutagenic bypass of canonical and atypical UV photoproducts," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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