Mechanistic Biology of Human Exonuclease-1-a DNA repair nuclease
Lead Research Organisation:
University of Sheffield
Department Name: Chemistry
Abstract
The ability to site-specifically hydrolyse
aberrant nucleic acids is essential to life. We
suggested that the 5'-nuclease superfamily achieve
this using a double nucleotide unpairing (DNU)
mechanism [1-2]. DNU is required for the scissile
phosphodiester (black dot) to contact active site ions
(blue). Working with the prototypical 5'-nuclease FEN1, we established novel
spectroscopic assays to visualize DNU [3]. We demonstrated that DNU requires
protein structural motifs that are distant from the active site [4]. This suggests the
potential to control DNU in vivo by alterations to protein structure tailored to
achieve biological specificity and/or regulation.
aberrant nucleic acids is essential to life. We
suggested that the 5'-nuclease superfamily achieve
this using a double nucleotide unpairing (DNU)
mechanism [1-2]. DNU is required for the scissile
phosphodiester (black dot) to contact active site ions
(blue). Working with the prototypical 5'-nuclease FEN1, we established novel
spectroscopic assays to visualize DNU [3]. We demonstrated that DNU requires
protein structural motifs that are distant from the active site [4]. This suggests the
potential to control DNU in vivo by alterations to protein structure tailored to
achieve biological specificity and/or regulation.
Organisations
People |
ORCID iD |
Studentship Projects
| Project Reference | Relationship | Related To | Start | End | Student Name |
|---|---|---|---|---|---|
| BB/M011151/1 | 30/09/2015 | 29/09/2023 | |||
| 2856422 | Studentship | BB/M011151/1 | 30/09/2015 | 29/09/2019 |