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Nucleic Acids Research, 2003, Vol. 31, No. 14 4024-4030
© 2003 Oxford University Press

Processing of DNA lesions by archaeal DNA polymerases from Sulfolobus solfataricus

Petr Grúz*,1, Masatomi Shimizu1,2, Francesca M. Pisani3, Mariarita De Felice3, Yusuke Kanke2 and Takehiko Nohmi1

1 Division of Genetics and Mutagenesis, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan, 2 Otsuma Women’s University, 12 Sanban-chou, Chiyoda-ku, Tokyo 102-8357, Japan and 3 Istituto di Biochimica delle Proteine ed Enzimologia, Consiglio Nazionale Ricerche, Via P. Castellino 111, Napoli 80131, Italy

*To whom correspondence should be addressed. Tel: +81 3 3700 9873; Fax: +81 3 3707 6950; Email: gruz{at}nihs.go.jp

Spontaneous damage to DNA as a result of deamination, oxidation and depurination is greatly accelerated at high temperatures. Hyperthermophilic microorganisms constantly exposed to temperatures exceeding 80°C are endowed with powerful DNA repair mechanisms to maintain genome stability. Of particular interest is the processing of DNA lesions during replication, which can result in fixed mutations. The hyperthermophilic crenarchaeon Sulfolobus solfataricus has two functional DNA polymerases, PolB1 and PolY1. We have found that the replicative DNA polymerase PolB1 specifically recognizes the presence of the deaminated bases hypoxanthine and uracil in the template by stalling DNA polymerization 3–4 bases upstream of these lesions and strongly associates with oligonucleotides containing them. PolB1 also stops at 8-oxoguanine and is unable to bypass an abasic site in the template. PolY1 belongs to the family of lesion bypass DNA polymerases and readily bypasses hypoxanthine, uracil and 8-oxoguanine, but not an abasic site, in the template. The specific recognition of deaminated bases by PolB1 may represent an initial step in their repair while PolY1 may be involved in damage tolerance at the replication fork. Additionally, we reveal that the deaminated bases can be introduced into DNA enzymatically, since both PolB1 and PolY1 are able to incorporate the aberrant DNA precursors dUTP and dITP.


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