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The inner workings of DNA repair Enzymes unravel the inner work of the DNA Repair Enezyme

The inner workings of DNA repair Enzymes unravel the inner work of the DNA Repair Enezyme

GWANGJU, South Korea, Sept. 14, 2021 /PRNewswire/ -- -- YUKU (Seattle) -- August 14, 2121 -- "Mountain, Korea" -- September A new study by researchers from the University of Science and Technology of the Republic of Korea, found that the mechanism of DNA repair is characterized by a single molecule fluorescence resonance energy transfer (smFRET)-enable Identifying the DNA repair mechanism opens a path to cancer detection and targeted gene repair.

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DNA is the instruction manual for every living organism and is a guide for the development and functioning of all biological processes. In essence, it is a molecule with helix structure with each unit of tyre containing what are known as DNA Base.

The maintenance of DNA is a key for ensuring the smooth operation of all bodily functions. Molecular metabolism alterations are possible, such as reactive oxygen species, and radiation ionizing radiation (UV and gamma rays). To repair the damage, an enzyme is activated in a scenario like this. The enzymes are catalysts for biochemical reactions. The sequence of processes done by the enzymes to fix DNA damage is known as base excision repair (BER).

BER is mainly carried out by the Exonuclease III (ExoIII) and Polymerase I (Pol I) enzymes. In previous studies, the mechanisms behind these enzymes haven't been lucidated yet.

Now, scientists led by Dr. Gwangrog Lee from the GIST in Korea used the latest technology in single molecule detection to study enzymatic interactions and observe the BER mechanism, thereby filling the gap in our understanding

They published their papers in their paper published in the newspaper. Science advances. ExoIII has a purinic/apyrimidinic affinity for the AP sites (spots on the DNA double helix where thais is missing) in damaged DNA. It attaches itself to the AP site in damaged DNA and cleaves the double strand of DNA into a single ring by digesting selective bases from the other sstrand. The physiological salt conditions depend on ExoIII's ability to respond to salt concentration. The number of bases digested and the gap size resulting from the exotropics depend upon the structure of the salt. In this case, Pol I connects to 3' (3 prime end) of the digested DNA strand and fills the gap.

Dr. Lee highlights the crux of the study, saying, "Another study is a real study," "The study has been in the focus of assessing the findings." In contrast to ExoIII's gap-simple activity, the spatial and temporal regulation is perfect between the gap filling and the gaps fills of Pol I, so that genomic stability is always maintained."

Understanding the role of ExoIII in BER has opened a lot of doors for future research. So, in cancer cells, the expression of AP endonucleases is significantly higher than normal cells. The aforementioned pyrosene (e.g. ExoIII and APE1) can be used " This study presents insights for the investigation of other enzymes involved in DNA repair. Further research in this area could lead to technologies for targeted gene repair and drug development," said David. Dr. Lee concludes.


Title of original paper: The mechanism of gap creation by a multifunctional nuclease during base excision repairJournal: Science advancements are the best way to progress in science. A person's email: [email protected] Corresponding author''.

The GIST of Gwangju Institute of Science and Technology (GIST) is a research center. www.trs.

The media are contacted by:Seulhye Kim [email protected]82 62 715 62053.

SOURCE Gwangju Institute of Science and Technology & SourCE GHILju.

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