TY - JOUR
T1 - Co-localization in replication foci and interaction of human Y-family members, DNA polymerase polη and REVl protein
AU - Tissier, Agnès
AU - Kannouche, Patricia
AU - Reck, Marie Pierre
AU - Lehmann, Alan R.
AU - Fuchs, Robert P.P.
AU - Cordonnier, Agnès
N1 - Funding Information:
This work was supported in part by an MRC Programme Grant to ARL and EU QoL Grant QLG-CT-1999-00181 to ARL and RPPF. We would like to thank all the members of the unit UPR 9003 for their helpful comments and suggestion during the course of this work; Jean-Baptiste Duvauchelle and Wassim Abdulrahman for their help in the construction of plasmids; Chris Lawrence and Peter Gibbs for providing pPGR1-1; Errol Friedberg and Valerie Gerlach for providing pGEM-T hDINBl; Roger Woodgate and John McDonald for providing clone 6-1; James Cleaver for XP30RO and Maria Cordeiro-Stone for CTag cell lines; and Fumio Hanaoka, Haruo Ohmori, Roger Woodgate and Errol Friedberg for generously sharing unpublished data prior to publication.
PY - 2004/11/2
Y1 - 2004/11/2
N2 - The progress of replicative DNA polymerases along the replication fork may be impeded by the presence of lesions in the genome. One way to circumvent such hurdles involves the recruitment of specialized DNA polymerases that perform limited incorporation of nucleotides in the vicinity of the damaged site. This process entails DNA polymerase switch between replicative and specialized DNA polymerases. Five eukaryotic proteins can carry out translesion synthesis (TLS) of damaged DNA in vitro, DNA polymerases ζ, η, ι, and κ, and REV1. To identify novel proteins that interact with hpolη, we performed a yeast two-hybrid screen. In this paper, we show that hREV1 interacts with hpolη as well as with hpolκ and poorly with hpolι. Furthermore, cellular localization analysis demonstrates that hREV1 is present, with hpolη in replication factories at stalled replication forks and is tightly associated with nuclear structures. This hREV1 nuclear localization occurs independently of the presence of hpolη. Taken together, our data suggest a central role for hREV1 as a scaffold that recruits DNA polymerases involved in TLS.
AB - The progress of replicative DNA polymerases along the replication fork may be impeded by the presence of lesions in the genome. One way to circumvent such hurdles involves the recruitment of specialized DNA polymerases that perform limited incorporation of nucleotides in the vicinity of the damaged site. This process entails DNA polymerase switch between replicative and specialized DNA polymerases. Five eukaryotic proteins can carry out translesion synthesis (TLS) of damaged DNA in vitro, DNA polymerases ζ, η, ι, and κ, and REV1. To identify novel proteins that interact with hpolη, we performed a yeast two-hybrid screen. In this paper, we show that hREV1 interacts with hpolη as well as with hpolκ and poorly with hpolι. Furthermore, cellular localization analysis demonstrates that hREV1 is present, with hpolη in replication factories at stalled replication forks and is tightly associated with nuclear structures. This hREV1 nuclear localization occurs independently of the presence of hpolη. Taken together, our data suggest a central role for hREV1 as a scaffold that recruits DNA polymerases involved in TLS.
KW - Translesion synthesis DNA polymerases
KW - hREV1
KW - hpolη
UR - http://www.scopus.com/inward/record.url?scp=4544251295&partnerID=8YFLogxK
U2 - 10.1016/j.dnarep.2004.06.015
DO - 10.1016/j.dnarep.2004.06.015
M3 - Article
C2 - 15380106
AN - SCOPUS:4544251295
SN - 1568-7864
VL - 3
SP - 1503
EP - 1514
JO - DNA Repair
JF - DNA Repair
IS - 11
ER -