Nucleic Acids Research, Vol 26, Issue 3 730-734, Copyright © 1998 by Oxford University Press
M Jokela, M Makiniemi, S Lehtonen, C Szpirer, U Hellman and JE Syvaoja
Human DNA polymerase epsilon is composed of a 261 kDa catalytic polypeptide
and a 55 kDa small subunit of unknown function. cDNAs encoding the small
subunit of human and mouse DNA polymerase epsilon were cloned. The
predicted polypeptides have molecular masses of 59.469 and 59.319 kDa
respectively and they are 90% identical. The human and mouse polypeptides
show 22% identity with the 80 kDa subunit of the five subunit DNA
polymerase epsilon from the yeast Saccharomyces cerevisiae. The high degree
of conservation suggests that the 55 kDa subunit shares an essential
function with the yeast 80 kDa subunit, which was earlier suggested to be
involved in S phase cell cycle control in a pathway that is able to sense
and signal incomplete replication. The small subunits of human and mouse
DNA polymerase epsilon also show homology to the C-terminal domain of the
second largest subunit of DNA polymerase alpha. The gene for the small
subunit of human DNA polymerase epsilon (POLE2) was localized to chromosome
14q21-q22 by fluorescence in situ hybridization.
ARTICLES
The small subunits of human and mouse DNA polymerase epsilon are homologous to the second largest subunit of the yeast Saccharomyces cerevisiae DNA polymerase epsilon
Biocenter Oulu and Department of Biochemistry, University of Oulu, FIN- 90570 Oulu, Finland.
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