Evidence map›Paper›PMID 21676997›Full record

ArticleNucleic acids research2011

A reverse transcriptase-related protein mediates phage resistance and polymerizes untemplated DNA in vitro.

Chen Wang, Manuela Villion, Cameron Semper, Colin Coros, Sylvain Moineau, Steven Zimmerly

Abstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

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  19. Expanding Diversity ofFrontiers in microbiology · 2021
    Article
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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

6 authors.

Chen WangDepartment of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
Manuela Villion
Cameron Semper
Colin Coros
Sylvain Moineau
Steven Zimmerly

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reverse transcriptases (RTs) are RNA-dependent DNA polymerases that usually function in the replication of selfish DNAs such as retrotransposons and retroviruses. Here, we have biochemically characterized a RT-related protein, AbiK, which is required for abortive phage infection in the Gram-positive bacterium Lactococcus lactis. In vitro, AbiK does not exhibit the properties expected for an RT, but polymerizes long DNAs of 'random' sequence, analogous to a terminal transferase. Moreover, the polymerized DNAs appear to be covalently attached to the AbiK protein, presumably because an amino acid serves as a primer. Mutagenesis experiments indicate that the polymerase activity resides in the RT motifs and is essential for phage resistance in vivo. These results establish a novel biochemical property and a non-replicative biological role for a polymerase.

Indexed as

Amino Acid MotifsAmino Acid SequenceBacterial ProteinsBacteriophagesDNADNA-Directed DNA PolymeraseLactococcus lactisMolecular Sequence DataMutationProtein Structure, TertiaryRNA-Directed DNA PolymeraseSequence Homology, Amino AcidAbiK protein, Lactococcus lactisBacterial ProteinsDNADNA-Directed DNA PolymeraseRNA-Directed DNA Polymerase

Identifiers

PMID21676997
PMCPMC3177184

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Registered trials

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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.