Evidence map›Paper›PMID 29055778›Full record

ArticleJournal of molecular biology2017

Structural Basis for the Persistence of Homing Endonucleases in Transcription Factor IIB Inteins.

Hideo Iwaï, Kornelia M Mikula, Jesper S Oeemig, Dongwen Zhou, Mi Li, Alexander Wlodawer

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-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

12 citing papers in PubMed, 18 citations in OpenAlex.

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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 at 3 institutions in 2 countries.

Hideo IwaïResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Helsinki FIN-00014, Finland. Electronic address: hideo.iwai@helsinki.fi.
Kornelia M MikulaResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Helsinki FIN-00014, Finland.
Jesper S OeemigResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Helsinki FIN-00014, Finland.
Dongwen ZhouMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Mi LiMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA; Basic Science Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.
Alexander WlodawerMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA. Electronic address: wlodawer@nih.gov.
University of Helsinki · FINational Cancer Institute · USLeidos (United States) · US

Funding

Protein StructureZIABC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2009 to 2025
$27.5M
CCR NIH HHS HHSN261200800001CIntramural NIH HHS ZIA BC010348NCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

Inteins are mobile genetic elements that are spliced out of proteins after translation. Some inteins contain a homing endonuclease (HEN) responsible for their propagation. Hedgehog/INTein (HINT) domains catalyzing protein splicing and their nested HEN domains are thought to be functionally independent because of the existence of functional mini-inteins without HEN domains. Despite the lack of obvious mutualism between HEN and HINT domains, HEN domains are persistently found at one specific site in inteins, indicating their potential functional role in protein splicing. Here we report crystal structures of inactive and active mini-inteins derived from inteins residing in the transcription factor IIB of Methanococcus jannaschii and Methanocaldococcus vulcanius, revealing a novel modified HINT fold that might provide new insights into the mutualism between the HEN and HINT domains. We propose an evolutionary model of inteins and a functional role of HEN domains in inteins.

Indexed as

InteinsAmino Acid SequenceCrystallography, X-RayEndonucleasesMethanococcusModels, MolecularProtein ConformationProtein SplicingSequence HomologyTranscription Factor TFIIBEndonucleasesTranscription Factor TFIIBhoming endonucleasehorizontal gene transferinteinsprotein splicing

Identifiers

PMID29055778
PMCPMC6309676
OpenAlexW2765778085

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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.