Evidence map›Paper›PMID 8255751›Full record

ArticleNucleic acids research1993

Evolutionary relationships among group II intron-encoded proteins and identification of a conserved domain that may be related to maturase function.

G Mohr, P S Perlman, A M Lambowitz

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
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

88 citing papers in PubMed, 214 citations in OpenAlex.

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  11. What viruses tell us about evolution and immunity: beyond Darwin?Annals of the New York Academy of Sciences · 2019
    Review
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  18. Functionality ofFrontiers in molecular biosciences · 2016
    Article
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  20. Article

28 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

G MohrDepartment of Molecular Genetics, Ohio State University, Columbus 43210.
P S Perlman
A M Lambowitz
The Ohio State University · USThe University of Texas Southwestern Medical Center · US

Funding

RETROPLASMID AND GROUP II INTRON REVERSE TRANSCRIPTASESR01GM037949 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2019
$8.6M
GENETIC AND MOLECULAR STUDIES OF RNA SPLICINGR01GM031480 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BUTOW, RONALD A · 1985 to 2004
$1.8M
NIGMS NIH HHS GM31480NIGMS NIH HHS GM37949
6 · The paper itself

Abstract

Many group II introns encode reverse transcriptase-like proteins that potentially function in intron mobility and RNA splicing. We compared 34 intron-encoded open reading frames and four related open reading frames that are not encoded in introns. Many of these open reading frames have a reverse transcriptase-like domain, followed by an additional conserved domain X, and a Zn(2+)-finger-like region. Some open reading frames have lost conserved sequence blocks or key amino acids characteristic of functional reverse transcriptases, and some lack the Zn(2+)-finger-like region. The open reading frames encoded by the chloroplast tRNA(Lys) genes and the related Epifagus virginiana matK open reading frame lack a Zn(2+)-finger-like region and have only remnants of a reverse transcriptase-like domain, but retain a readily identifiable domain X. Several findings lead us to speculate that domain X may function in binding of the intron RNA during reverse transcription and RNA splicing. Overall, our findings are consistent with the hypothesis that all of the known group II intron open reading frames evolved from an ancestral open reading frame, which contained reverse transcriptase, X, and Zn(2+)-finger-like domains, and that the reverse transcriptase and Zn(2+)-finger-like domains were lost in some cases. The retention of domain X in most proteins may reflect an essential function in RNA splicing, which is independent of the reverse transcriptase activity of these proteins.

Indexed as

Biological EvolutionIntronsAmino Acid SequenceBinding SitesChloroplastsConserved SequenceEndoribonucleasesMolecular Sequence DataNucleotidyltransferasesOpen Reading FramesPlantsProteinsRNA, Transfer, LysSequence Homology, Amino AcidEndoribonucleasesmRNA maturaseNucleotidyltransferasesProteinsRNA, Transfer, Lys

Identifiers

PMID8255751
PMCPMC310608
OpenAlexW2020556436

What OpenQuestion holds

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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.