Nucleic Acids Research, Vol 27, Issue 21 4235-4240, Copyright © 1999 by Oxford University Press
OI Lavrik, DM Kolpashchikov, K Weisshart, HP Nasheuer, SN Khodyreva and A Favre
To analyze the interaction of human replication protein A (RPA) and its
subunits with the DNA template-primer junction in the DNA replication fork,
we designed several template-primer systems differing in the size of the
single-stranded template tail (4, 9, 13, 14, 19 and 31 nt). Base
substituted photoreactive dNTP analogs-5-[ N -(2-nitro-5-azidobenzoyl)-
trans -3-amino-propenyl-1]-2'-deoxyuridine-5'-triphosphate (NAB-4-dUTP) and
5-[ N -[ N -(2-nitro-5-azidobenzoyl)glycyl]- trans -3-aminopropenyl-
1]-2'-deoxyuridine-5'-triphosphate (NAB-7-dUTP)-were used as substrates for
elongation of radiolabeled primer-template by DNA polymerases in the
presence or absence of RPA. Subsequent UV crosslinking showed that the
pattern of p32 and p70 RPA subunit labeling, and consequently their
interaction with the template-primer junction, is strongly dependent on the
template extension length at a particular RPA concentration, as well as on
the ratio of RPA to template concentration. Our results suggest a model of
changes in the RPA configuration modulating by the length of the template
extension in the course of nascent DNA synthesis.
ARTICLES
RPA subunit arrangement near the 3'-end of the primer is modulated by the length of the template strand and cooperative protein interactions
Novosibirsk Institute of Bioorganic Chemistry Siberian Division of Russian Academy of Sciences, Prospect Lavrentiev 8, 630090 Novosibirsk, Russia. lavrik@niboch.nsc.ru
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