Article ; Online: The enzymatic properties of Arabidopsis thaliana DNA polymerase λ suggest a role in base excision repair.
2024 Volume 114, Issue 1, Page(s) 3
Abstract: Base excision repair (BER) generates gapped DNA intermediates containing a 5'-terminal 2-deoxyribose-5-phosphate (5'-dRP) group. In mammalian cells, gap filling and dRP removal are catalyzed by Pol β, which belongs to the X family of DNA polymerases. In ... ...
Abstract | Base excision repair (BER) generates gapped DNA intermediates containing a 5'-terminal 2-deoxyribose-5-phosphate (5'-dRP) group. In mammalian cells, gap filling and dRP removal are catalyzed by Pol β, which belongs to the X family of DNA polymerases. In higher plants, the only member of the X family of DNA polymerases is Pol λ. Although it is generally believed that plant Pol λ participates in BER, there is limited experimental evidence for this hypothesis. Here we have characterized the biochemical properties of Arabidopsis thaliana Pol λ (AtPol λ) in a BER context, using a variety of DNA repair intermediates. We have found that AtPol λ performs gap filling inserting the correct nucleotide, and that the rate of nucleotide incorporation is higher in substrates containing a C in the template strand. Gap filling catalyzed by AtPol λ is most efficient with a phosphate at the 5'-end of the gap and is not inhibited by the presence of a 5'-dRP mimic. We also show that AtPol λ possesses an intrinsic dRP lyase activity that is reduced by mutations at two lysine residues in its 8-kDa domain, one of which is present in Pol λ exclusively and not in any Pol β homolog. Importantly, we also found that the dRP lyase activity of AtPol λ allows efficient completion of uracil repair in a reconstituted short-patch BER reaction. These results suggest that AtPol λ plays an important role in plant BER. |
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MeSH term(s) | Animals ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Excision Repair ; DNA-Directed DNA Polymerase/genetics ; DNA-Directed DNA Polymerase/chemistry ; DNA-Directed DNA Polymerase/metabolism ; DNA Repair ; Nucleotides ; Phosphates ; Mammals/metabolism ; DNA Polymerase beta |
Chemical Substances | DNA polymerase beta2 (EC 2.7.7.-) ; DNA-Directed DNA Polymerase (EC 2.7.7.7) ; Nucleotides ; Phosphates ; DNA Polymerase beta (EC 2.7.7.7) |
Language | English |
Publishing date | 2024-01-13 |
Publishing country | Netherlands |
Document type | Journal Article |
ZDB-ID | 778032-1 |
ISSN | 1573-5028 ; 0167-4412 |
ISSN (online) | 1573-5028 |
ISSN | 0167-4412 |
DOI | 10.1007/s11103-023-01407-8 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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