Structural highlights
Publication Abstract from PubMed
Replicative DNA polymerases are highly efficient enzymes that maintain stringent geometric control over shape and orientation of the template and incoming nucleoside triphosphate. In a surprising twist to this paradigm, a naturally occurring bacterial DNA polymerase I member isolated from Geobacillus stearothermophilus (Bst) exhibits an innate ability to reverse transcribe RNA and other synthetic congeners (XNAs) into DNA. This observation raises the interesting question of how a replicative DNA polymerase is able to recognize templates of diverse chemical composition. Here, we present crystal structures of natural Bst DNA polymerase that capture the post-translocated product of DNA synthesis on templates composed entirely of 2'-deoxy-2'-fluoro-beta-d-arabino nucleic acid (FANA) and alpha-l-threofuranosyl nucleic acid (TNA). Analysis of the enzyme active site reveals the importance of structural plasticity as a possible mechanism for XNA-dependent DNA synthesis and provides insights into the construction of variants with improved activity.
Crystal structures of a natural DNA polymerase that functions as an XNA reverse transcriptase.,Jackson LN, Chim N, Shi C, Chaput JC Nucleic Acids Res. 2019 Jun 6. pii: 5512092. doi: 10.1093/nar/gkz513. PMID:31170294[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jackson LN, Chim N, Shi C, Chaput JC. Crystal structures of a natural DNA polymerase that functions as an XNA reverse transcriptase. Nucleic Acids Res. 2019 Jun 6. pii: 5512092. doi: 10.1093/nar/gkz513. PMID:31170294 doi:http://dx.doi.org/10.1093/nar/gkz513
