Nucleic Acids Research, 2000, Vol. 28, No. 18 3684-3693
© 2000 Oxford University Press
Two novel human and mouse DNA polymerases of the polX family
INSERM U373, Faculté de Médecine Necker-Enfants Malades, Université Paris V, 156 rue de Vaugirard, 75730 Paris cedex 15, France
We describe here two novel mouse and human DNA polymerases: one (pol 
) has homology with DNA polymerase ß while the other one (pol µ) is closer to terminal deoxynucleotidyltransferase. However both have DNA polymerase activity in vitro and share similar structural organization, including a BRCT domain, helix–loop–helix DNA-binding motifs and polymerase X domain. mRNA expression of pol is highest in testis and fetal liver, while expression of pol µ is more lymphoid, with highest expression both in thymus and tonsillar B cells. An unusually large number of splice variants is observed for the pol µ gene, most of which affect the polymerase domain. Expression of mRNA of both polymerases is down-regulated upon treatment by DNA damaging agents (UV light, 
-rays or H2O2). This suggests that their biological function may differ from DNA translesion synthesis, for which several DNA polymerase activities have been recently described. Possible functions are discussed.
* To whom correspondence should be addressed. Tel: +33 1 40 61 56 83; Fax: +33 1 40 61 55 90; Email: reynaud@infobiogen.fr Present addresses: Laurentiu Cocea, Amgen Research Institute, 620 University Avenue, Suite 706, Toronto, Ontario M5G 2C1, Canada Neetu Gupta, CNRS UMR 1773, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris cedex 15, France +AF161019, AF176097, AF176098 and AF176099
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