Evidence map›Paper›PMID 15574519›Full record

ArticleRNA (New York, N.Y.)2005

Domain structure and three-dimensional model of a group II intron-encoded reverse transcriptase.

Forrest J H Blocker, Georg Mohr, Lori H Conlan, Li Qi, Marlene Belfort, Alan M Lambowitz

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

63 citing papers in PubMed, 94 citations in OpenAlex.

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3 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

6 authors at 2 institutions in 1 country.

Forrest J H BlockerInstitute for Cellular and Molecular Biology, University of Texas at Austin, 1 University Station A4800, Austin, TX 78712, USA.
Georg Mohr
Lori H Conlan
Li Qi
Marlene Belfort
Alan M Lambowitz
New York State Department of Health · USThe University of Texas at Austin · US

Funding

SELF-SPLICING INTEINS: FUNCTION, EVOLUTION, APPLICATIONR01GM044844 · NIGMS · WADSWORTH CENTER · PI BELFORT, MARLENE · 1990 to 2019
$8.9M
RETROPLASMID AND GROUP II INTRON REVERSE TRANSCRIPTASESR01GM037949 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2019
$8.6M
RNA SPLICING IN NEUROSPORA MITOCHONDRIAR01GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2016
$6.6M
SELF-SPLICING INTRONS IN THE PHAGE T4/E COLI SYSTEMR01GM039422 · NIGMS · WADSWORTH CENTER · PI BELFORT, MARLENE · 1988 to 2019
$5.3M
INTRON DYNAMICS IN BACTERIAR37GM039422 · NIGMS · WADSWORTH CENTER · PI BELFORT, MARLENE · 2001 to 2010
$4.0M
INVOLVEMENT OF PROTEINS IN SPLICING GROUP I INTRONSR37GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1993 to 2002
$1.2M
NIGMS NIH HHS GM06837NIGMS NIH HHS GM37949NIGMS NIH HHS GM37951NIGMS NIH HHS GM39422NIGMS NIH HHS GM44844NIGMS NIH HHS R01 GM037949NIGMS NIH HHS R01 GM037951NIGMS NIH HHS R01 GM039422NIGMS NIH HHS R01 GM044844NIGMS NIH HHS R37 GM037951NIGMS NIH HHS R37 GM039422
6 · The paper itself

Abstract

Group II intron-encoded proteins (IEPs) have both reverse transcriptase (RT) activity, which functions in intron mobility, and maturase activity, which promotes RNA splicing by stabilizing the catalytically active RNA structure. The LtrA protein encoded by the Lactococcus lactis Ll.LtrB group II intron contains an N-terminal RT domain, with conserved sequence motifs RT1 to 7 found in the fingers and palm of retroviral RTs; domain X, associated with maturase activity; and C-terminal DNA-binding and DNA endonuclease domains. Here, partial proteolysis of LtrA with trypsin and Arg-C shows major cleavage sites in RT1, and between the RT and X domains. Group II intron and related non-LTR retroelement RTs contain an N-terminal extension and several insertions relative to retroviral RTs, some with conserved features implying functional importance. Sequence alignments, secondary-structure predictions, and hydrophobicity profiles suggest that domain X is related structurally to the thumb of retroviral RTs. Three-dimensional models of LtrA constructed by "threading" the aligned sequence on X-ray crystal structures of HIV-1 RT (1) account for the proteolytic cleavage sites; (2) suggest a template-primer binding track analogous to that of HIV-1 RT; and (3) show that conserved regions in splicing-competent LtrA variants include regions of the RT and X (thumb) domains in and around the template-primer binding track, distal regions of the fingers, and patches on the protein's back surface. These regions potentially comprise an extended RNA-binding surface that interacts with different regions of the intron for RNA splicing and reverse transcription.

Indexed as

Amino Acid SequenceBacterial ProteinsBase SequenceBinding SitesGenes, BacterialHIV-1HIV Reverse TranscriptaseIntronsLactococcus lactisModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryRetroelementsRNA, BacterialBacterial ProteinsHIV Reverse TranscriptaseLtrA protein, Lactococcus lactisRetroelementsRNA, BacterialRNA-Directed DNA Polymerase

Identifiers

PMID15574519
PMCPMC1370687
OpenAlexW2046975919

What OpenQuestion holds

Textmetadata
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.