Human RECQL5beta stimulates flap endonuclease 1
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Human RECQL5beta stimulates flap endonuclease 1. / Speina, Elzbieta; Dawut, Lale; Hedayati, Mohammad; Wang, Zhengming; May, Alfred; Schwendener, Sybille; Janscak, Pavel; Croteau, Deborah L; Bohr, Vilhelm A.
In: Nucleic Acids Symposium Series, Vol. 38, No. 9, 01.05.2010, p. 2904-16.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Human RECQL5beta stimulates flap endonuclease 1
AU - Speina, Elzbieta
AU - Dawut, Lale
AU - Hedayati, Mohammad
AU - Wang, Zhengming
AU - May, Alfred
AU - Schwendener, Sybille
AU - Janscak, Pavel
AU - Croteau, Deborah L
AU - Bohr, Vilhelm A
PY - 2010/5/1
Y1 - 2010/5/1
N2 - Human RECQL5 is a member of the RecQ helicase family which is implicated in genome maintenance. Five human members of the family have been identified; three of them, BLM, WRN and RECQL4 are associated with elevated cancer risk. RECQL1 and RECQL5 have not been linked to any human disorder yet; cells devoid of RECQL1 and RECQL5 display increased chromosomal instability. Here, we report the physical and functional interaction of the large isomer of RECQL5, RECQL5beta, with the human flap endonuclease 1, FEN1, which plays a critical role in DNA replication, recombination and repair. RECQL5beta dramatically stimulates the rate of FEN1 cleavage of flap DNA substrates. Moreover, we show that RECQL5beta and FEN1 interact physically and co-localize in the nucleus in response to DNA damage. Our findings, together with the previous literature on WRN, BLM and RECQL4's stimulation of FEN1, suggests that the ability of RecQ helicases to stimulate FEN1 may be a general feature of this class of enzymes. This could indicate a common role for the RecQ helicases in the processing of oxidative DNA damage.
AB - Human RECQL5 is a member of the RecQ helicase family which is implicated in genome maintenance. Five human members of the family have been identified; three of them, BLM, WRN and RECQL4 are associated with elevated cancer risk. RECQL1 and RECQL5 have not been linked to any human disorder yet; cells devoid of RECQL1 and RECQL5 display increased chromosomal instability. Here, we report the physical and functional interaction of the large isomer of RECQL5, RECQL5beta, with the human flap endonuclease 1, FEN1, which plays a critical role in DNA replication, recombination and repair. RECQL5beta dramatically stimulates the rate of FEN1 cleavage of flap DNA substrates. Moreover, we show that RECQL5beta and FEN1 interact physically and co-localize in the nucleus in response to DNA damage. Our findings, together with the previous literature on WRN, BLM and RECQL4's stimulation of FEN1, suggests that the ability of RecQ helicases to stimulate FEN1 may be a general feature of this class of enzymes. This could indicate a common role for the RecQ helicases in the processing of oxidative DNA damage.
KW - Cell Line
KW - Cell Nucleus
KW - DNA
KW - DNA Cleavage
KW - DNA, Single-Stranded
KW - Flap Endonucleases
KW - Humans
KW - RecQ Helicases
U2 - 10.1093/nar/gkp1217
DO - 10.1093/nar/gkp1217
M3 - Journal article
C2 - 20081208
VL - 38
SP - 2904
EP - 2916
JO - Nucleic acids symposium series
JF - Nucleic acids symposium series
SN - 0261-3166
IS - 9
ER -
ID: 33491872