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

Chikahide Masutani, Rika Kusumoto, Ayumi Yamada, Naoshi Dohmae, Masayuki Yokoi, Mayumi Yuasa, Marito Araki, Shigenori Iwai, Koji Takio and Fumio Hanaoka ()
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Chikahide Masutani: Institute for Molecular and Cellular Biology, Osaka University
Rika Kusumoto: Institute for Molecular and Cellular Biology, Osaka University
Ayumi Yamada: Institute for Molecular and Cellular Biology, Osaka University
Naoshi Dohmae: Institute of Physical and Chemical Research (RIKEN)
Masayuki Yokoi: Institute for Molecular and Cellular Biology, Osaka University
Mayumi Yuasa: Institute for Molecular and Cellular Biology, Osaka University
Marito Araki: Institute for Molecular and Cellular Biology, Osaka University
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

Nature, 1999, vol. 399, issue 6737, 700-704

Abstract: 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.

Date: 1999
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DOI: 10.1038/21447

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