Evidence map›Paper›PMID 23827238›Full record

ArticleBiochimica et biophysica acta2013

Zar1 represses translation in Xenopus oocytes and binds to the TCS in maternal mRNAs with different characteristics than Zar2.

Tomomi M Yamamoto, Jonathan M Cook, Cassandra V Kotter, Terry Khat, Kevin D Silva, Michael Ferreyros, Justin W Holt, Jefferson D Knight, Amanda Charlesworth

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

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  8. Sex Lethal Gene Manipulates Gonadal Development of Medaka,International journal of molecular sciences · 2022
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  13. Maternal variants inJournal of medical genetics · 2018
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  14. Review
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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

9 authors at 2 institutions in 1 country.

Tomomi M YamamotoDepartment of Integrative Biology, University of Colorado Denver, Denver, CO, USA. Electronic address: tomomi.yamamoto@ucdenver.edu.
Jonathan M Cook
Cassandra V Kotter
Terry Khat
Kevin D Silva
Michael Ferreyros
Justin W Holt
Jefferson D Knight
Amanda Charlesworth
University of Colorado Denver · USUniversity of Arkansas for Medical Sciences · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Telemedicine CoreP30GM110702 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI GARCIA-RILL, EDGAR E. · 2014 to 2018
$6.1M
Center for Translational NeuroscienceP20GM103425 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI GARCIA-RILL, EDGAR E. · 2012 to 2013
$4.1M
Evolution of interactions between Wolbachia and its hosts: Drosophila model systeR01GM104325 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI TURELLI, MICHAEL · 2013 to 2016
$1.6M
NCI NIH HHS P30 CA046934NIGMS NIH HHS P20 GM103425NIGMS NIH HHS P20 GM104325NIGMS NIH HHS P30 GM110702NIGMS NIH HHS R01 GM104325
6 · The paper itself

Abstract

Maternal mRNAs are translationally regulated during early development. Zar1 and its closely related homolog, Zar2, are both crucial in early development. Xenopus laevis Zygote arrest 2 (Zar2) binds to the Translational Control Sequence (TCS) in maternal mRNAs and regulates translation. The molecular mechanism of Zar1 has not been described. Here we report similarities and differences between Xenopus Zar1 and Zar2. Analysis of Zar sequences in vertebrates revealed two Zar family members with conserved, characteristic amino acid differences in the C-terminal domain. The presence of only two vertebrate Zar proteins was supported by analyzing Zar1 synteny. We propose that the criteria for naming Zar sequences are based on the characteristic amino acids and the chromosomal context. We also propose reclassification of some Zar sequences. We found that Zar1 is expressed throughout oogenesis and is stable during oocyte maturation. The N-terminal domain of Zar1 repressed translation of a reporter construct in immature oocytes. Both Zar1 and Zar2 bound to the TCS in the Wee1 and Mos 3' UTRs using a zinc finger in the C-terminal domain. However, Zar1 had much higher affinity for RNA than Zar2. To show the functional significance of the conserved amino acid substitutions, these residues in Zar2 were mutated to those found in Zar1. We show that these residues contributed to the different RNA binding characteristics of Zar1 compared to Zar2. Our study shows that Zar proteins have generally similar molecular functions in the translational regulation of maternal mRNAs, but they may have different roles in early development.

Indexed as

Protein BiosynthesisAmino Acid SequenceAnimalsCell Cycle ProteinsCells, CulturedGene Expression Regulation, DevelopmentalMolecular Sequence DataOocytesOogenesisProtein-Tyrosine KinasesRNA, Messenger, StoredSequence Homology, Amino AcidXenopus laevisXenopus ProteinsCell Cycle ProteinsProtein-Tyrosine KinasesRNA, Messenger, StoredWEE1 protein, XenopusXenopus ProteinsZar2 protein, XenopusCPECPEBcytoplasmic polyadenylation elementcytoplasmic polyadenylation element binding proteinelectrophoretic mobility shift assayEMSAMBEMusashi binding elementRNA binding proteinTCSTranslational controlTranslational Control Sequenceuntranslated regionUTRXenopus oocyteZygote arrest

Identifiers

PMID23827238
PMCPMC3810179
OpenAlexW2060265196

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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.