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Protein-templated synthesis of dinucleotide repeat DNA by an antiphage reverse transcriptase.

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Title: Protein-templated synthesis of dinucleotide repeat DNA by an antiphage reverse transcriptase.
Authors: Deng, Pujuan (AUTHOR), Lee, Hyunbin (AUTHOR), Armijo, Carlo (AUTHOR), Wang, Haoqing (AUTHOR), Gao, Alex (AUTHOR)
Source: Science. 6/18/2026, Vol. 392 Issue 6804, p1274-1281. 8p.
Subjects: DNA synthesis, Reverse transcriptase, Polymerization, Microsatellite repeats, Non-coding RNA
Abstract: Defense-associated reverse transcriptases (DRTs) are widespread bacterial antiphage systems that use unconventional mechanisms of polynucleotide synthesis. We show that DRT3, which comprises two distinct RTs (Drt3a and Drt3b) and a noncoding RNA (ncRNA), synthesizes alternating poly(GT/AC) double-stranded DNA. Cryo–electron microscopy structures at 2.6-angstrom resolution reveal a D3-symmetric 6:6:6 complex of Drt3a, Drt3b, and ncRNA. Drt3a produces the poly(GT) strand using a conserved ACACAC template within the ncRNA. Notably, Drt3b synthesizes a complementary, protein-primed poly(AC) strand in the complete absence of a nucleic acid template, using conserved active site residues specific to Drt3b to enforce precise base alternation. These findings expand the functional landscape of nucleic acid polymerases, revealing a protein-templated mechanism for sequence-specific DNA synthesis. Editor's summary: Bacterial defense systems often deploy unconventional biochemistry to thwart viral infection. Investigating the antiphage system DRT3, Deng et al. found that it defends against infection by synthesizing repetitive poly(GT/AC) double-stranded DNA using two distinct reverse transcriptases (RTs). One of its RTs copies a noncoding RNA, and the second synthesizes the complementary DNA strand de novo without any nucleic acid template. Instead, it uses its own amino acids as a physical mold to enforce precise base alternation. This work reveals a surprising protein-templated mechanism for sequence-specific DNA synthesis, expanding the known repertoire of enzymatic polymerization. —Di Jiang [ABSTRACT FROM AUTHOR]
Copyright of Science is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Group: Ti
  Data: Protein-templated synthesis of dinucleotide repeat DNA by an antiphage reverse transcriptase.
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  Data: <searchLink fieldCode="AR" term="%22Deng%2C+Pujuan%22">Deng, Pujuan</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lee%2C+Hyunbin%22">Lee, Hyunbin</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Armijo%2C+Carlo%22">Armijo, Carlo</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wang%2C+Haoqing%22">Wang, Haoqing</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Gao%2C+Alex%22">Gao, Alex</searchLink> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Science%22">Science</searchLink>. 6/18/2026, Vol. 392 Issue 6804, p1274-1281. 8p.
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  Data: <searchLink fieldCode="DE" term="%22DNA+synthesis%22">DNA synthesis</searchLink><br /><searchLink fieldCode="DE" term="%22Reverse+transcriptase%22">Reverse transcriptase</searchLink><br /><searchLink fieldCode="DE" term="%22Polymerization%22">Polymerization</searchLink><br /><searchLink fieldCode="DE" term="%22Microsatellite+repeats%22">Microsatellite repeats</searchLink><br /><searchLink fieldCode="DE" term="%22Non-coding+RNA%22">Non-coding RNA</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Defense-associated reverse transcriptases (DRTs) are widespread bacterial antiphage systems that use unconventional mechanisms of polynucleotide synthesis. We show that DRT3, which comprises two distinct RTs (Drt3a and Drt3b) and a noncoding RNA (ncRNA), synthesizes alternating poly(GT/AC) double-stranded DNA. Cryo–electron microscopy structures at 2.6-angstrom resolution reveal a D3-symmetric 6:6:6 complex of Drt3a, Drt3b, and ncRNA. Drt3a produces the poly(GT) strand using a conserved ACACAC template within the ncRNA. Notably, Drt3b synthesizes a complementary, protein-primed poly(AC) strand in the complete absence of a nucleic acid template, using conserved active site residues specific to Drt3b to enforce precise base alternation. These findings expand the functional landscape of nucleic acid polymerases, revealing a protein-templated mechanism for sequence-specific DNA synthesis. Editor's summary: Bacterial defense systems often deploy unconventional biochemistry to thwart viral infection. Investigating the antiphage system DRT3, Deng et al. found that it defends against infection by synthesizing repetitive poly(GT/AC) double-stranded DNA using two distinct reverse transcriptases (RTs). One of its RTs copies a noncoding RNA, and the second synthesizes the complementary DNA strand de novo without any nucleic acid template. Instead, it uses its own amino acids as a physical mold to enforce precise base alternation. This work reveals a surprising protein-templated mechanism for sequence-specific DNA synthesis, expanding the known repertoire of enzymatic polymerization. —Di Jiang [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Science is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1126/science.aed1656
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        Text: English
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      – SubjectFull: Polymerization
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      – SubjectFull: Microsatellite repeats
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              Text: 6/18/2026
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              Y: 2026
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