Abstract
Translesion synthesis past an oxidized abasic site, 2-deoxyribonolactone, in Escherichia coli results in high levels of dG incorporation and is dependent upon DNA polymerase V (Pol V). Kinetic experiments performed here affirm that Pol V preferentially incorporates dG opposite 2-deoxyribonolactone (L). Pol V discriminates between dG and dA on the basis of the apparent KD, suggesting that L provides instructive structural information to the enzyme despite lacking a Watson-Crick base.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
