TY - JOUR
T1 - Two novel human and mouse DNA polymerases of the poIX family
AU - Aoufouchi, Said
AU - Flatter, Eric
AU - Dahan, Auriel
AU - Faili, Ahmad
AU - Bertocci, Barbara
AU - Storck, Sebastien
AU - Delbos, Frédéric
AU - Cocea, Laurentiu
AU - Gupta, Neetu
AU - Weill, Jean Claude
AU - Reynaud, Claude Agnès
PY - 2000/9/15
Y1 - 2000/9/15
N2 - We describe here two novel mouse and human DNA polymerases: one (pol λ) has homology with DNA polymerase β 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 λ 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, γ-rays or H202. 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.
AB - We describe here two novel mouse and human DNA polymerases: one (pol λ) has homology with DNA polymerase β 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 λ 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, γ-rays or H202. 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.
UR - http://www.scopus.com/inward/record.url?scp=0034666193&partnerID=8YFLogxK
M3 - Article
C2 - 10982892
AN - SCOPUS:0034666193
SN - 0305-1048
VL - 28
SP - 3684
EP - 3693
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 18
ER -