Ontology highlight
ABSTRACT:
SUBMITTER: Aoufouchi S
PROVIDER: S-EPMC110747 | biostudies-literature | 2000 Sep
REPOSITORIES: biostudies-literature
Aoufouchi S S Flatter E E Dahan A A Faili A A Bertocci B B Storck S S Delbos F F Cocea L L Gupta N N Weill J C JC Reynaud C A CA
Nucleic acids research 20000901 18
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 ...[more]