The 3′–5′ exonucleases

@article{Shevelev2002The3E,
  title={The 3′–5′ exonucleases},
  author={Igor V. Shevelev and Ulrich Hübscher},
  journal={Nature Reviews Molecular Cell Biology},
  year={2002},
  volume={3},
  pages={364-376}
}
Over the past few years, several new 3′–5′ exonucleases have been identified. In vitro studies of these enzymes have uncovered much about their potential functions in vivo, and certain organisms with a defect in 3′–5′ exonucleases have an increased susceptibility to cancer, especially under conditions of stress. Here, we look at not only the newly discovered enzymes, but also at the roles of other 3′–5′ exonucleases in the quality control of DNA synthesis, where they act as proofreading… 

The Multiple Biological Roles of the 3′→5′ Exonuclease of Saccharomyces cerevisiae DNA Polymerase δ Require Switching between the Polymerase and Exonuclease Domains

It is concluded that the three biological functions of the 3′→5′ exonuclease addressed in this study are performed intramolecularly within the replicating holoenzyme.

A Novel Single-Strand Specific 3′–5′ Exonuclease Found in the Hyperthermophilic Archaeon, Pyrococcus furiosus

A novel nuclease may be involved in a DNA repair pathway conserved in the living organisms as a specific member for some hyperthermophilic archaea, and lacks similarity to any other proteins with known function, including hitherto reported 3′–5′ exonucleases.

A 3′-5′ exonuclease activity embedded in the helicase core domain of Candida albicans Pif1 helicase

It is uncovered that Candida albicans Pif1 (CaPif1) displays a 3′-5′ exonuclease activity besides its main helicase activity, which may suggest a biochemical basis for mechanistic studies of Pif 1 family helicases.

Modulation of the 3′→5′-Exonuclease Activity of Human Apurinic Endonuclease (Ape1) by Its 5′-incised Abasic DNA Product*

Roles for the Ape1 exonuclease during BER are suggested after both DNA repair synthesis and excision of the abasic deoxyribose-5-phosphate by polymerase β.

The Presence of 3′–5′ Exonuclease Activity in Rat Brain Neurons and Its Role in Template-Driven Extension of 3′-Mismatched Primers by DNA-Polymerase β in Aging Neurons

The results revealed that in the case of duplexes with a mismatch at 3′-end of primer, significant extension by DNA polymerase β has taken place only after the removal of the mismatched base, thus indicating the presence of a proof reading 3′–5′ exonuclease activity in neuronal extracts of all ages.

The Human TREX2 3′ → 5′-Exonuclease Structure Suggests a Mechanism for Efficient Nonprocessive DNA Catalysis*

The human TREX2 catalytic residues overlay with the bacterial DnaQ family of 3′-exonucleases confirming the structural conservation of the catalytic sites despite limited sequence identity, and mutations of these residues decrease the still measurable activity by ∼105-fold, confirming their catalytic role.

Ratio of 3′ → 5′-exonuclease and DNA polymerase activities in normal and cancer cells of rodents and human

In experiments on cells growing in culture, it has been found that in adult human dermal fibroblasts the value of ratio of activity of 3′ → 5′-exonucleases to the DNA polymerase activity (3′- exo/pol) exceeds this ratio for HeLa cells.

A sequence-dependent exonuclease activity from Tetrahymena thermophila

The specificities of the enzyme indicate that this novel Tetrahymena exonuclease is distinct from Exo1 and has properties required for 3'-overhang formations at telomeres.

3′-End Polishing of the Kinetoplastid Spliced Leader RNA Is Performed by SNIP, a 3′→5′ Exonuclease with a Motley Assortment of Small RNA Substrates

The identification and characterization of a nonexosomal, 3′→5′ exonuclease required for SL RNA 3′-end formation in Trypanosoma brucei is reported and it is speculated that SNIP is part of an organized nucleoplasmic machinery responsible for processing of SL RNA.

[Antimutagenic role of autonomous 3'-->5'-exonucleases].

An investigation of thirty objects from all three kingdoms of life has shown that AE increase significantly the intracellular ratio of 3′ → 5′-exonuclease to DNA polymerase activities in a wide phylogenetic variety of species, which always leads to the increasing fidelity of DNA biosynthesis.
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