Evidence map›Paper›PMID 21115847›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Targeted insertion of cysteine by decoding UGA codons with mammalian selenocysteine machinery.

Xue-Ming Xu, Anton A Turanov, Bradley A Carlson, Min-Hyuk Yoo, Robert A Everley, Renu Nandakumar, Irina Sorokina, Steven P Gygi, Vadim N Gladyshev, Dolph L Hatfield

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

53 citing papers in PubMed, 87 citations in OpenAlex.

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  13. Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022
    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

10 authors at 6 institutions in 1 country.

Xue-Ming XuMolecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Anton A Turanov
Bradley A Carlson
Min-Hyuk Yoo
Robert A Everley
Renu Nandakumar
Irina Sorokina
Steven P Gygi
Vadim N Gladyshev
Dolph L Hatfield
Harvard University · USNational Institutes of Health · USBrigham and Women's Hospital · USCenter for Cancer Research · USNational Cancer Institute · USUniversity of Nebraska–Lincoln · US

Funding

IDENTITY OF TERMINATOR AND SELENOCYSTEINE UGA CODONSR01GM061603 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2000 to 2016
$4.0M
Functions of thioredoxin reductases and their targetsR37GM065204 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI GLADYSHEV, VADIM N. · 2011 to 2020
$4.0M
Functions of Mammalian Thioredoxin ReductasesR01GM065204 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2002 to 2009
$2.2M
Biosynthesis of Selenocysteine and Its Incorporation into ProteinZIABC010767 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HATFIELD, DOLPH · 2009 to 2014
$2.0M
Intramural NIH HHSNIGMS NIH HHS GM061603NIGMS NIH HHS GM065204NIGMS NIH HHS R01 GM061603NIGMS NIH HHS R01 GM065204NIGMS NIH HHS R37 GM065204
6 · The paper itself

Abstract

Cysteine (Cys) is inserted into proteins in response to UGC and UGU codons. Herein, we show that supplementation of mammalian cells with thiophosphate led to targeted insertion of Cys at the UGA codon of thioredoxin reductase 1 (TR1). This Cys was synthesized by selenocysteine (Sec) synthase on tRNA([Ser]Sec) and its insertion was dependent on the Sec insertion sequence element in the 3'UTR of TR1 mRNA. The substrate for this reaction, thiophosphate, was synthesized by selenophosphate synthetase 2 from ATP and sulfide and reacted with phosphoseryl-tRNA([Ser]Sec) to generate Cys-tRNA([Ser]Sec). Cys was inserted in vivo at UGA codons in natural mammalian TRs, and this process was regulated by dietary selenium and availability of thiophosphate. Cys occurred at 10% of the Sec levels in liver TR1 of mice maintained on a diet with normal amounts of selenium and at 50% in liver TR1 of mice maintained on a selenium deficient diet. These data reveal a novel Sec machinery-based mechanism for biosynthesis and insertion of Cys into protein at UGA codons and suggest new biological functions for thiophosphate and sulfide in mammals.

Indexed as

Codon, TerminatorAnimalsCysteineDietIsoenzymesLiverMiceMice, Inbred C57BLMutagenesis, InsertionalNIH 3T3 CellsPhosphatesRNA, Transfer, Amino AcylSeleniumSelenocysteineThioredoxin Reductase 1TransferasesCodon, TerminatorCysteineIsoenzymesPhosphatesRNA, Transfer, Amino AcylSeleniumselenium transferaseSelenocysteinethiophosphoric acidThioredoxin Reductase 1Transferases

Identifiers

PMID21115847
PMCPMC3003055
OpenAlexW2020986313

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.