Evidence map›Paper›PMID 31170294›Full record

ArticleNucleic acids research2019

Crystal structures of a natural DNA polymerase that functions as an XNA reverse transcriptase.

Lynnette N Jackson, Nicholas Chim, Changhua Shi, John C Chaput

Abstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  2. Article
  3. The XNA alphabet.Nucleic acids research · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Thermophilic Nucleic Acid Polymerases and Their Application in Xenobiology.International journal of molecular sciences · 2022
    Review
  9. Crystal structure of DNA polymerase I from Thermus phage G20c.Acta crystallographica. Section D, Structural biology · 2022
    Article
  10. Article
  11. Loop-Mediated Isothermal Amplification: From Theory to Practice.Russian journal of bioorganic chemistry · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. In Vitro Selection of an ATP-Binding TNA Aptamer.Molecules (Basel, Switzerland) · 2020
    Article
  17. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Lynnette N JacksonDepartments of Pharmaceutical Sciences, University of California, Irvine, CA 92697-3958, USA.
Nicholas ChimDepartments of Pharmaceutical Sciences, University of California, Irvine, CA 92697-3958, USA.
Changhua ShiDepartments of Pharmaceutical Sciences, University of California, Irvine, CA 92697-3958, USA.
John C ChaputDepartments of Pharmaceutical Sciences, University of California, Irvine, CA 92697-3958, USA.

Funding

MINORITY BIOMEDICAL RESEARCHERS PROGRAMR25GM055246 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI MOTA-BRAVO, LUIS M · 1996 to 2022
$15.3M
MARC U*STAR at the University of California, IrvineT34GM069337 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI BUCHMEIER, MICHAEL JOSEPH, DE LA CRUZ, MARLENE · 2005 to 2019
$8.2M
NIGMS NIH HHS R25 GM055246NIGMS NIH HHS T34 GM069337
6 · The paper itself

Abstract

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-β-d-arabino nucleic acid (FANA) and α-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.

Indexed as

ArabinonucleotidesBacterial ProteinsCatalytic DomainCrystallography, X-RayDNA, BacterialDNA Polymerase IGeobacillus stearothermophilusModels, MolecularNucleic Acid HybridizationNucleosidesNucleotidesProtein BindingProtein ConformationRNA-Directed DNA PolymeraseStructure-Activity RelationshipTemplates, Genetic2'-deoxy-2'-fluoro-beta-D-arabinonucleic acidalpha-L-threofuranosyl nucleoside triphosphateArabinonucleotidesBacterial ProteinsDNA, BacterialDNA Polymerase INucleosidesNucleotidesRNA-Directed DNA Polymerase

Identifiers

PMID31170294
PMCPMC6649750

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.