Open AccessTwo novel human and mouse DNA polymerases of the polX family
Author(s) -
Saïd Aoufouchi,
Eric Flatter,
Auriel Dahan,
Ahmad Faili,
Barbara Bertocci,
Sébastien Storck,
Frédéric Delbos,
Laurentiu Cocea,
Neetu Gupta,
JeanClaude Weill,
ClaudeAgnès Reynaud
Publication year - 2000
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/28.18.3684
Subject(s) - biology , dna polymerase , dna polymerase mu , dna polymerase ii , polymerase , microbiology and biotechnology , dna clamp , dna polymerase delta , processivity , dna polymerase i , genetics , dna , gene , reverse transcriptase , circular bacterial chromosome , polymerase chain reaction
We describe here two novel mouse and human DNA polymerases: one (pol lambda) has homology with DNA polymerase beta while the other one (pol mu) 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 lambda is highest in testis and fetal liver, while expression of pol mu 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 mu 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, gamma-rays or H(2)O(2)). 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.