Evidence map›Paper›PMID 35708663›Full record

ArticleG3 (Bethesda, Md.)2022

Isha is a su(Hw) mRNA-binding protein required for gypsy insulator function.

Indira Bag, Yang Chen, Karole D'Orazio, Prisma Lopez, Sabine Wenzel, Yuichiro Takagi, Elissa P Lei

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in G3 (Bethesda, Md.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

7 authors.

Indira BagNuclear Organization and Gene Expression Section, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.ORCID 0000-0002-5491-5869
Yang ChenNuclear Organization and Gene Expression Section, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.ORCID 0000-0003-0147-3443
Karole D'OrazioNuclear Organization and Gene Expression Section, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Prisma LopezNuclear Organization and Gene Expression Section, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Sabine WenzelDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Yuichiro TakagiDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.ORCID 0000-0002-0988-6798
Elissa P LeiNuclear Organization and Gene Expression Section, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.ORCID 0000-0003-4894-0037

Funding

Chromatin Insulator Function and Nuclear OrganizationZIADK015602 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI LEI, ELISSA · 2009 to 2025
$24.7M
Mechanism of transcription regulation by the MediatorR01GM111695 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI TAKAGI, YUICHIRO · 2015 to 2019
$1.5M
NIGMS NIH HHS R01 GM111695
6 · The paper itself

Abstract

Chromatin insulators are DNA-protein complexes localized throughout the genome capable of establishing independent transcriptional domains. It was previously reported that the Drosophila su(Hw) mRNA physically associates with the gypsy chromatin insulator protein complex within the nucleus and may serve a noncoding function to affect insulator activity. However, how this mRNA is recruited to the gypsy complex is not known. Here, we utilized RNA-affinity pulldown coupled with mass spectrometry to identify a novel RNA-binding protein, Isha (CG4266), that associates with su(Hw) mRNA in vitro and in vivo. Isha harbors a conserved RNA recognition motif and RNA Polymerase II C-terminal domain-interacting domain (CID). We found that Isha physically interacts with total and elongating Polymerase II and associates with chromatin at the 5' end of genes in an RNA-dependent manner. Furthermore, ChIP-seq analysis reveals Isha overlaps particularly with the core gypsy insulator component CP190 on chromatin. Depletion of Isha reduces enhancer-blocking and barrier activities of the gypsy insulator and disrupts the nuclear localization of insulator bodies. Our results reveal a novel factor Isha that promotes gypsy insulator activity that may act as a nuclear RNA-binding protein adapter for su(Hw) noncoding mRNA.

Indexed as

Drosophila ProteinsAnimalsCarrier ProteinsChromatinDNA-Binding ProteinsDrosophilaDrosophila melanogasterMicrotubule-Associated ProteinsNuclear ProteinsRepressor ProteinsRNA-Binding ProteinsRNA, MessengerCarrier ProteinsChromatinCP190 protein, DrosophilaDNA-Binding ProteinsDrosophila ProteinsMicrotubule-Associated ProteinsNuclear ProteinsRepressor ProteinsRNA-Binding ProteinsRNA, Messengerbarrier activityCG4266chromatinDrosophilaenhancer blockinggypsyinsulatornoncoding mRNARNA bindingsu(Hw)

Identifiers

PMID35708663
PMCPMC9434307

What OpenQuestion holds

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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.