Human exonuclease 1 (EXO1) activity characterization and its function on FLAP structures
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Human exonuclease 1 (EXO1) activity characterization and its function on FLAP structures. / Keijzers, Guido; Bohr, Vilhelm A; Juel Rasmussen, Lene.
In: Bioscience Reports, Vol. 35, No. 3, e00206, 2015.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Human exonuclease 1 (EXO1) activity characterization and its function on FLAP structures
AU - Keijzers, Guido
AU - Bohr, Vilhelm A
AU - Juel Rasmussen, Lene
PY - 2015
Y1 - 2015
N2 - Human exonuclease 1 (EXO1) is involved in multiple DNA metabolism processes, including DNA repair and replication. Most of the fundamental roles of EXO1 have been described in yeast. Here, we report a biochemical characterization of human full-length EXO1. Prior to assay EXO1 on different DNA flap structures, we determined factors essential for the thermodynamic stability of EXO1. We show that enzymatic activity and stability of EXO1 on DNA is modulated by temperature. By characterization of EXO1 flap activity using various DNA flap substrates, we show that EXO1 has a strong capacity for degrading double stranded DNA and has a modest endonuclease or 5' flap activity. Furthermore, we report novel mechanistic insights into the processing of flap structures, showing that EXO1 preferentially cleaves one nucleotide inwards in a double stranded region of a forked and nicked DNA flap substrates, suggesting a possible role of EXO1 in strand displacement.
AB - Human exonuclease 1 (EXO1) is involved in multiple DNA metabolism processes, including DNA repair and replication. Most of the fundamental roles of EXO1 have been described in yeast. Here, we report a biochemical characterization of human full-length EXO1. Prior to assay EXO1 on different DNA flap structures, we determined factors essential for the thermodynamic stability of EXO1. We show that enzymatic activity and stability of EXO1 on DNA is modulated by temperature. By characterization of EXO1 flap activity using various DNA flap substrates, we show that EXO1 has a strong capacity for degrading double stranded DNA and has a modest endonuclease or 5' flap activity. Furthermore, we report novel mechanistic insights into the processing of flap structures, showing that EXO1 preferentially cleaves one nucleotide inwards in a double stranded region of a forked and nicked DNA flap substrates, suggesting a possible role of EXO1 in strand displacement.
U2 - 10.1042/BSR20150058
DO - 10.1042/BSR20150058
M3 - Journal article
C2 - 25913924
VL - 35
JO - Bioscience Reports
JF - Bioscience Reports
SN - 0144-8463
IS - 3
M1 - e00206
ER -
ID: 138734282