TY - JOUR
T1 - Characterization of a UV endonuclease gene from the fisson yeast Schizosaccharomyces pombe and its bacterial homolog
AU - Takao, Masashi
AU - Yonemasu, Rie
AU - Yamamoto, Kazuo
AU - Yasui, Akira
N1 - Funding Information:
We would like to thank Drs Takeshi Todo and Andries P.M. Eker for providing us with Drosophila and Anacystis photolyases, respectively. The presence of nucleotide sequence in theBacillus database homologous to a part of the UVDE gene ofN.crassa was first informed by Dr Paul W. Doetsch, for which we are very grateful. Technical assistance by Ms Izumi Chiba and Ms Junko Kikuchi is acknowledged. This work was supported by a Grant-in-Aid for Scientific Research on Priority Area No. 07270101 from the Ministry of Education, Science, Sports and Culture of Japan to A. Yasui.
PY - 1996
Y1 - 1996
N2 - From the fission yeast Schizosaccharomyces pombe, a cDNA fragment was isolated, which confers UV resistance on repair deficient Escherichia coli host cells. The cloned cDNA encodes a protein of 68 815 Da, which has a 36.6% identity of amino acid sequence with the previously identified 74 kDa UV endonuclease of the filamentous fungus Neurospora crassa. Analysis of several truncated gene constructs shows that only the C-terminal two thirds region, which has 54% identity of amino acid sequence with the C-terminal region of the Neurospora homolog, is necessary for complementing activity of UV-sensitivity in the E.coli host cells. Purified recombinant protein from E.coli host cells incises both UV-induced cyclobutane pyrimidine dimers and (6-4) photoproducts at the sites immediately 5' to the DNA damage in the same fashion as the Neurospora protein. Furthermore, a bacterial homologous sequence was isolated from Bacillus subtilis and shows a similar complementing activity of UV sensitivity in E.coli host cells, indicating a wide distribution of this alternative excision repair mechanism in life.
AB - From the fission yeast Schizosaccharomyces pombe, a cDNA fragment was isolated, which confers UV resistance on repair deficient Escherichia coli host cells. The cloned cDNA encodes a protein of 68 815 Da, which has a 36.6% identity of amino acid sequence with the previously identified 74 kDa UV endonuclease of the filamentous fungus Neurospora crassa. Analysis of several truncated gene constructs shows that only the C-terminal two thirds region, which has 54% identity of amino acid sequence with the C-terminal region of the Neurospora homolog, is necessary for complementing activity of UV-sensitivity in the E.coli host cells. Purified recombinant protein from E.coli host cells incises both UV-induced cyclobutane pyrimidine dimers and (6-4) photoproducts at the sites immediately 5' to the DNA damage in the same fashion as the Neurospora protein. Furthermore, a bacterial homologous sequence was isolated from Bacillus subtilis and shows a similar complementing activity of UV sensitivity in E.coli host cells, indicating a wide distribution of this alternative excision repair mechanism in life.
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U2 - 10.1093/nar/24.7.1267
DO - 10.1093/nar/24.7.1267
M3 - Article
C2 - 8614629
AN - SCOPUS:0029989496
VL - 24
SP - 1267
EP - 1271
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 7
ER -