Nucleic Acids Research, Vol 26, Issue 17 3877-3882, Copyright © 1998 by Oxford University Press
BL Allen, F Uhlmann, LK Gaur, BA Mulder, KL Posey, LB Jones and SH Hardin
Replication Factor C (RFC) is a five-subunit protein complex required for
eukaryotic DNA replication and repair. The large subunit within this
complex contains a C-terminal DNA binding domain which provides specificity
for PCNA loading at a primer-template and a second, N- terminal DNA binding
domain of unknown function. We isolated the N- terminal DNA binding domain
from Drosophila melanogaster and defined the region within this polypeptide
required for DNA binding. The DNA determinants most efficiently recognized
by both the Drosophila minimal DNA binding domain and the N-terminal half
of the human large subunit consist of a double-stranded DNA containing a
recessed 5' phosphate. DNA containing a recessed 5' phosphate was preferred
5-fold over hairpined DNA containing a recessed 3' hydroxyl. Combined with
existing data, these DNA binding properties suggest a role for the
N-terminal DNA binding domain in the recognition of phosphorylated DNA
ends.
ARTICLES
DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C
Department of Biology, Texas A&M University, College Station, TX 77843, USA.
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