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Information on EC 3.1.11.1 - exodeoxyribonuclease I and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39875
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3.1.11.1 exodeoxyribonuclease ISpecify your search results
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- 3.1.11.1
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphodiesterase, dna polymerase i, exonuclease i, exonuclease 1, exo i, hexo1, polb1, 3'-to-5' exonuclease, sbcb15, drpase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'5' exonuclease
-
-
-
-
DNA deoxyribophosphodiesterase
-
-
-
-
dRPase
-
-
-
-
E. coli exonuclease I
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-
-
-
Escherichia coli exonuclease I
-
-
-
-
exonuclease I
additional information
-
Exo1 is a member of the Rad2 protein family
exonuclease I
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9037-46-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicked circular single stranded DNA containing mismatches + H2O
?
-
-
-
?
nicked double stranded DNA containing mismatches + H2O
?
-
-
-
?
mismatched DNA + H2O
?
-
the enzyme shows 5' to 3' exonuclease activity
-
-
?
damaged DNA + H2O
?
-
requirement of the Mre11 complex and exonuclease 1, playing overlapping roles, for activation of the Mec1 signaling pathway, Mre11 and Exo1 collaborate in producing long single-stranded DNA tails at double-strand breaks of DNA and promote Mec1 association with the double-strand break, Mre11 and Exo1 contribute to the activation of the replication checkpoint pathway, modeling of complex activity
-
-
?
damaged DNA + H2O
?
-
the enzyme possesses 5' to 3' exonuclease activity and acts in the Mre11 complex producing long single-stranded DNA tails at double-strand breaks of DNA
-
-
?
additional information
?
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme is part of the mismatch repair complex, Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective rad53 mutant cells by resecting newly synthesized chains and resolving the sister chromatid junctions that cause regression of collapsed forks, mechanism modeling, overview
-
-
?
additional information
?
-
-
Exo1 is involved in 5' strand resection. Sgs1 and Exo1 can act independently to remove the 5' strand. Exo1 promotes resection in the absence of Dna2. Dna2 and Exo1 nucleases process 5' strands at a DSB
-
-
?
additional information
?
-
-
yeast Exo1 interacts with human MLH1 through its Mlh1 interacting protein box (R-SK-[Y/F]-F-motif). A mutant of MLH1 targeted at site S2 (Mlh1-E682A) behaves as a hypomorphic form of Exo1. The site S2 in Mlh1 mediates Exo1 recruitment in order to optimize mismatch repair-dependent mutation avoidance
-
-
?
additional information
?
-
-
Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicked circular single stranded DNA containing mismatches + H2O
?
-
-
-
?
nicked double stranded DNA containing mismatches + H2O
?
-
-
-
?
damaged DNA + H2O
?
-
requirement of the Mre11 complex and exonuclease 1, playing overlapping roles, for activation of the Mec1 signaling pathway, Mre11 and Exo1 collaborate in producing long single-stranded DNA tails at double-strand breaks of DNA and promote Mec1 association with the double-strand break, Mre11 and Exo1 contribute to the activation of the replication checkpoint pathway, modeling of complex activity
-
-
?
additional information
?
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme is part of the mismatch repair complex, Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective rad53 mutant cells by resecting newly synthesized chains and resolving the sister chromatid junctions that cause regression of collapsed forks, mechanism modeling, overview
-
-
?
additional information
?
-
-
Exo1 is involved in 5' strand resection. Sgs1 and Exo1 can act independently to remove the 5' strand. Exo1 promotes resection in the absence of Dna2. Dna2 and Exo1 nucleases process 5' strands at a DSB
-
-
?
additional information
?
-
-
yeast Exo1 interacts with human MLH1 through its Mlh1 interacting protein box (R-SK-[Y/F]-F-motif). A mutant of MLH1 targeted at site S2 (Mlh1-E682A) behaves as a hypomorphic form of Exo1. The site S2 in Mlh1 mediates Exo1 recruitment in order to optimize mismatch repair-dependent mutation avoidance
-
-
?
additional information
?
-
-
Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
-
-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
enzyme-deficient exo1DELTA yeast cells repairing plasmids with 5'-extensions can produce repair junction with templated insertions. Exo1D mutants have a reduced median size of deletions when joining DNA with blunt ends, and exo1D pol4D mutants repair blunt ends with a very low frequency of deletions, phenotypes, overview
malfunction
-
nearly all double-strand breaks are converted to chromosome breaks in cells lacking both exonuclease 1 activity and RAD50/MRE11/XRS2, MRX, complex
physiological function
-
DNA processing or resection carried out in the presence of Exo1 is efficient at preventing the double-strand break to chromosome break transition and that the exonuclease activity associated with exonuclease 1 plays a major role. Some feature of exonuclease processing or resection at a double-strand break is critical for maintaining broken chromosome ends in close proximity, additional role for Exo1 of maintaining chromosome continuity upon introduction of a double-strand break
physiological function
-
Exo1 acts at a late stage in end-processing during non-homologous end-joining, NHEJ. Exo1 can reverse nucleotide additions occurring due to polymerization, and may also be important for processing ends to expose microhomologies needed for NHEJ. Acurate joining is controlled at two steps, a first step that blocks mdification of DNA ends, which requires Tdp1, and a second step that occurs after synapsis that requires Exo1, overview
physiological function
-
in addition to performing a variety of functions during mitotic growth, Exo1 is also important for the production of crossovers during meiosis, the nuclease activity of exonuclease I is essential for normal 5'-3' resection at the Spo11-dependent HIS4 hotspot in otherwise wild-type cells. This same activity is also required for normal levels of gene conversion at the locus. Exo1 also plays a nuclease-independent role in crossover promotion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cotta-Ramusino, C.; Fachinetti, D.; Lucca, C.; Doksani, Y.; Lopes, M.; Sogo, J.; Foiani, M.
Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective cells
Mol. Cell
17
153-159
2005
Saccharomyces cerevisiae
Nakada, D.; Hirano, Y.; Sugimoto, K.
Requirement of the Mre11 complex and exonuclease 1 for activation of the Mec1 signaling pathway
Mol. Cell. Biol.
24
10016-10025
2004
Saccharomyces cerevisiae
Tran, P.T.; Fey, J.P.; Erdeniz, N.; Gellon, L.; Boiteux, S.; Liskay, R.M.
A mutation in EXO1 defines separable roles in DNA mismatch repair and post-replication repair
DNA Repair
6
1572-1583
2007
Saccharomyces cerevisiae (P39875)
Zhu, Z.; Chung, W.H.; Shim, E.Y.; Lee, S.E.; Ira, G.
Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends
Cell
134
981-994
2008
Saccharomyces cerevisiae
Segurado, M.; Diffley, J.F.
Separate roles for the DNA damage checkpoint protein kinases in stabilizing DNA replication forks
Genes Dev.
22
1816-1827
2008
Saccharomyces cerevisiae
Dherin, C.; Gueneau, E.; Francin, M.; Nunez, M.; Miron, S.; Liberti, S.E.; Rasmussen, L.J.; Zinn-Justin, S.; Gilquin, B.; Charbonnier, J.B.; Boiteux, S.
Characterization of a highly conserved binding site of Mlh1 required for exonuclease I-dependent mismatch repair
Mol. Cell. Biol.
29
907-918
2009
Saccharomyces cerevisiae, Homo sapiens
Nakai, W.; Westmoreland, J.; Yeh, E.; Bloom, K.; Resnick, M.A.
Chromosome integrity at a double-strand break requires exonuclease 1 and MRX
DNA Repair
10
102-110
2011
Saccharomyces cerevisiae
Keelagher, R.E.; Cotton, V.E.; Goldman, A.S.; Borts, R.H.
Separable roles for exonuclease I in meiotic DNA double-strand break repair
DNA Repair
10
126-137
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae SK1
Bahmed, K.; Seth, A.; Nitiss, K.C.; Nitiss, J.L.
End-processing during non-homologous end-joining: a role for exonuclease 1
Nucleic Acids Res.
39
970-978
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Goellner, E.M.; Putnam, C.D.; Kolodner, R.D.
Exonuclease 1-dependent and independent mismatch repair
DNA Repair
32
24-32
2015
Saccharomyces cerevisiae (P39875), Saccharomyces cerevisiae, Homo sapiens (Q9UQ84), Homo sapiens
Wang, W.; Daley, J.M.; Kwon, Y.; Xue, X.; Krasner, D.S.; Miller, A.S.; Nguyen, K.A.; Williamson, E.A.; Shim, E.Y.; Lee, S.E.; Hromas, R.; Sung, P.
A DNA nick at Ku-blocked double-strand break ends serves as an entry site for exonuclease 1 (Exo1) or Sgs1-Dna2 in long-range DNA end resection
J. Biol. Chem.
293
17061-17069
2018
Saccharomyces cerevisiae (P39875), Saccharomyces cerevisiae
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