Nucleic Acids Research, Vol 27, Issue 11 2361-2368, Copyright © 1999 by Oxford University Press
N Suzuki, M Shiratori, M Goto and Y Furuichi
We show that WRN helicase contains a unique 5'-->3' exonuclease activity
in the N-terminal region. Adeletion mutant lacking 231 N- terminal amino
acid residues, made in a baculovirus system, did nothave this activity,
while it showed ATPase and DNA helicase activities. This exonuclease
activity was co-precipitated with the helicase activity using monoclonal
antibodies specific to WRN helicase, indicating that it is an integral
component with WRN helicase. The exonuclease in WRN helicase does not
digest free single-stranded DNA or RNA, but it digests a strand in the
duplex DNA or an RNA strand in a RNA/DNA heteroduplex in a 5'-->3'
direction dependent on duplex unwinding. The digestion products were
identified as 5'-mononucleotides. Our data show that WRN helicase needs a
single-stranded 3' overhang region for efficient binding and unwinding of
duplex molecules, while blunt-ended or 5' overhang duplex molecules were
hardly unwound. These findings suggest that the WRN helicase and integral
5'-->3' exonuclease activities are involved in preventing a
hyper-recombination by resolving entangled structures of DNA and RNA/DNA
heteroduplexes that may be generated during rep-lication, repair and/or
transcription.
ARTICLES
Werner syndrome helicase contains a 5'-->3' exonuclease activity that digests DNA and RNA strands in DNA/DNA and RNA/DNA duplexes dependent on unwinding
AGENE Research Institute, 200 Kajiwara, Kamakura 247-0063, Japan.
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