Open AccessStructural relationship between DNA polymerases ε and ε⋆and their occurence in eukaryotic cells
Author(s) -
Lahja Uitto,
Jussi M. Halleen,
Teuvo Hentunen,
Matti Höyhtyä,
Juhani E. Syväoja
Publication year - 1995
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/23.2.244
Subject(s) - dna polymerase , biology , dna clamp , dna polymerase ii , polymerase , microbiology and biotechnology , dna polymerase i , dna polymerase mu , dna polymerase delta , primer (cosmetics) , dna , biochemistry , polymerase chain reaction , circular bacterial chromosome , gene , reverse transcriptase , chemistry , organic chemistry
Monoclonal antibodies raised against the N-terminal half of human DNA polymerase epsilon bind both to a large > 200 kDa form of DNA polymerase epsilon from HeLa cells and to a small 140 kDa form (DNA polymerase epsilon*) from calf thymus, while antibody against the C-terminal half binds to DNA polymerase epsilon but does not bind to DNA polymerase epsilon*. These results indicate that the two enzymes have common structural motifs in their N-terminal halves, and that DNA polymerase epsilon* is very likely derived from DNA polymerase epsilon by removal of its C-terminal half. DNA polymerase epsilon as well as DNA polymerase epsilon* was detected in extracts from cells of numerous eukaryotic species from yeast to human. The results indicate that DNA polymerase epsilon and its tendency to occur in a smaller form, DNA polymerase epsilon*, are evolutionarily highly conserved and that DNA polymerase epsilon may occur universally in proliferating eukaryotic cells.