Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D319A
does not alter the secondary structure significantly. 2-fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
E150A
does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
E318A
does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
K227A
does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
L331A
does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
Q311A
does not alter the secondary structure significantly. Displays modest 2fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R148A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R316A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R327A
does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R338A
does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
Y207A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
A153V
the mutation is associated with colorectal cancer and cancer of the small intestine
E109K
the mutation is associated with colorectal cancer
E589K
the mutation is associated with gastric cancer, lung cancer, hepatocellular carcinoma, melanoma, and glioblastoma
E670G
the mutation is associated with gastric cancer, breast cancer, oral cancer, lung cancer, melanoma, and glioblastoma
F506A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
F507A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
N279S
the mutation is associated with breast cancer and pancreatic cancer
P757L
the mutation is associated with colorectal cancer, pancreatic cancer, gastric cancer, breast cancer, oral cancer, lung cancer, and melanoma
Q154A/Y157A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
Q285A/F288A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
R723G/R723S
the mutation is associated with gastric cancer, breast cancer, oral cancer, and lung cancer
S504A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
T439M
the mutation is associated with colorectal cancer
D368A
-
the exonuclease-deficient mutant is drastically impaired for 3'-to-5' exonuclease activity, with no activity detected even at high enzyme-to-DNA substrate ratios
D405A
-
mutant enzyme loses 99.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity
D405E
-
mutant enzyme loses 95.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity
DELTAH672-S775
-
mutant enzyme loses 99% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity
DELTAL717-S775
-
mutant enzyme loses 97% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity
DELTAL746-S775
-
mutant protein has DNA polymerizing activity with 2.3fold higher specific activity than that of the wild-type but retains only 10% of the 3'->5' exonucleolytic activity of the wild-type
D173A
-
site-directed mutagenesis, the exo1-D173A mutant defective in nuclease activity is able to maintain crossing-over at wild-type levels in a number of genetic intervals. Exo1-D173A cells are able to maintain crossing-over despite reducedhDNAformation
F447A
-
abolishes binding to human MLH1
F448A
-
abolishes binding to human MLH1
S445A
-
abolishes binding to human MLH1
D173A
-
site-directed mutagenesis, the exo1-D173A mutant defective in nuclease activity is able to maintain crossing-over at wild-type levels in a number of genetic intervals. Exo1-D173A cells are able to maintain crossing-over despite reducedhDNAformation
-
D173A
-
with either mutant D173A alone or both mutant D173A and BLM, nucleolytic degradation is undetectable. It competitively inhibits Exo1-BLM-mediated resection
D173A
inactive mutant, structure in complex with Ca2+, overview
F506A/F507A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
F506A/F507A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
additional information
-
mutant lacking RecJ, ExoI, ExoVII and ExoX exonucleases abolishes normal mismatch repair in vitro but confers only a modest increase in mutation rate
additional information
-
the quadruple mutant lacking RecJ, ExoI, ExoVII and ExoX exonucleases and the triple mutant lacking RecJ, ExoI and ExoVII are characterized by sensitivity to the base analogous 2-aminopurine. The quadruple mutant displays a cold-sensitive phenotype and is unable to form colonies at 30°C on rich medium
additional information
-
in RecBCD+ cells, a mutated single-strand DNA 3'-5' exonuclease ExoI induces an increase in stationary-phase mutation. In sbcB15 cells, as in wild-type cells, these mutations partially require RecA, RecB, RecF, and expression of the LexA regulon. Absence of ExoI (DELTAxon) in wild-type or sbcC cells does not change significantly the stationary-phase mutation
additional information
analysis of single- and multiple-point mutants reveals that mutation to Ala of the three hydroxyurea-induced sites of phosphorylation partially rescues hydroxyurea-dependent degradation of hEXO1 and additionally stabilizes the protein in non-treated cells
additional information
-
analysis of single- and multiple-point mutants reveals that mutation to Ala of the three hydroxyurea-induced sites of phosphorylation partially rescues hydroxyurea-dependent degradation of hEXO1 and additionally stabilizes the protein in non-treated cells
additional information
-
various DNA damage phenotypes in response to camptothecin occur after siRNA-mediated downregulation of CtIP and EXO1
additional information
-
construction of enzyme-deficient mutant mice which show a deficient humoral response and immunoglobulin switching defects, the mutant mice show altered patterns of somatic hypermutation, overview
additional information
-
switch junction position is altered in Exo1-/- mice
additional information
generation of a mutant enzyme that is defective for the function of Exo1p in DNA mismatch repair due to disrupted interaction with Mlh1p, but still functional for post-replication repair
additional information
-
exo1DELTA but not mlh1-E682A presents significant increase in canavanin-resistant mutant events. Mlh1-R547A exo1DELTA and mlh1-E682A exo1DELTA double mutants show that mlh1-R547A synergistically interacts with exo1DELTA, yielding high canavanin-resistant forward and Hom+ reversion mutation rates, whereas mlh1-E682A does not
additional information
-
initiation of resection in exo1DELTA mutant cells is comparable to that in wild-type cells. In exo1DELTA sgs1DELTA double mutants, the Mre11-Rad50-Xrs2 complex together with Sae2 nuclease generate, in a stepwise manner, only few hundred nucleotides of ssDNA at the break, resulting in inefficient gene conversion and G2/M damage checkpoint arrest. Resection in sgs1DELTA exo1DELTA is limited to the vicinity of double-strand break ends and depends on the Mre11-Rad50-Xrs2 complex and Sae2. G2/M checkpoint arrest in response to a single double-strand break is impaired in sgs1D exo1D cells
additional information
-
sensitivity of rad53 mutants to DNA-damaging agents can be almost completely suppressed by deletion of the EXO1 gene. Deletion of EXO1 also suppresses DNA replication fork instability in rad53 mutants. Deletion of EXO1 is completely ineffective in suppressing both the sensitivity and replication fork breakdown in mec1 mutants
additional information
-
when the exo1DELTA or the exo1-D173A nuclease mutations are combined with a rad50DELTA mutation, the frequency of large budded cells with a CRB following I-SceI induction increases to 80% or 65% with HO, induction of CRBs by HO-endonuclease is also increased in an exo1DELTA mutant