tailieunhanh - Báo cáo khoa học: Purification, cDNA cloning, and expression profiles of the cyclobutane pyrimidine dimer photolyase of Xenopus laevis

Photolyase is a light-dependent enzyme that repairs pyrimidine dimers in DNA. Two types of photolyases have been found in frogXenopus laevis, one for repairing cyclobutane pyrimidine dimers (CPD photolyase) and the other for pyrimidine–pyrimidone (6–4)photoproduct [(6–4)photolyase]. However, little is known about the former type of theXenopusphotolyases. | iFEBS Journal Purification cDNA cloning and expression profiles of the cyclobutane pyrimidine dimer photolyase of Xenopus laevis Hiroaki Tanida Eiji Tahara Miwa Mochizuki Yukiko Yamane and Masaru Ryoji Laboratory of Molecular Biology Department of Life Sciences PrefecturalUniversity of Hiroshima Hiroshima Japan Keywords affinity purification cDNA cloning cyclobutane pyrimidine dimer photolyase Xenopus laevis Correspondence M. Ryoji Laboratory of Molecular Biology Department of Life Sciences Prefectural University of Hiroshima 562 Nanatsuka Shobara Hiroshima 727-0023 Japan Tel Fax 81 824 74 1755 E-mail ryoji@ Present address Wakunaga PharmaceuticalCo. Ltd 1624 Shimokotachi Koda-cho Takata-gun Hiroshima 739-1195 Japan Note The sequence and the alignment reported in this paper are available in the DDBJ EMBL GenBank databases under the accession numbers AB175838 and ALIGN_000880. Photolyase is a light-dependent enzyme that repairs pyrimidine dimers in DNA. Two types of photolyases have been found in frog Xenopus laevis one for repairing cyclobutane pyrimidine dimers CPD photolyase and the other for pyrimidine-pyrimidone 6-4 photoproduct 6-4 photolyase . However little is known about the former type of the Xenopus photolyases. To characterize this enzyme and its expression profiles we isolated the entire coding region of a putative CPD photolyase cDNA by extending an EST expressed sequence tag sequence obtained from the Xenopus database. Nucleotide sequence analysis of the cDNA revealed a protein of 557 amino acids with close similarity to CPD photolyase of rat kangaroo. The identity of this cDNA was further established by the molecular mass 65 kDa and the partial amino acid sequences of the major CPD photolyase that we purified from Xenopus ovaries. The gene of this enzyme is expressed in various tissues of Xenopus. Even internal organs like heart express relatively high levels of mRNA. A much smaller amount was found in skin although UV damage is .

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