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The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data. / Babaylova, Elena S.; Kolobova, Alena V.; Gopanenko, Alexander V. и др.

в: Biochimie, Том 177, 01.10.2020, стр. 68-77.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Babaylova, ES, Kolobova, AV, Gopanenko, AV, Tupikin, AE, Kabilov, MR, Malygin, AA & Karpova, GG 2020, 'The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data', Biochimie, Том. 177, стр. 68-77. https://doi.org/10.1016/j.biochi.2020.07.019

APA

Babaylova, E. S., Kolobova, A. V., Gopanenko, A. V., Tupikin, A. E., Kabilov, M. R., Malygin, A. A., & Karpova, G. G. (2020). The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data. Biochimie, 177, 68-77. https://doi.org/10.1016/j.biochi.2020.07.019

Vancouver

Babaylova ES, Kolobova AV, Gopanenko AV, Tupikin AE, Kabilov MR, Malygin AA и др. The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data. Biochimie. 2020 окт. 1;177:68-77. doi: 10.1016/j.biochi.2020.07.019

Author

Babaylova, Elena S. ; Kolobova, Alena V. ; Gopanenko, Alexander V. и др. / The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data. в: Biochimie. 2020 ; Том 177. стр. 68-77.

BibTeX

@article{da7da819ab30479392dea3ee24dc16e6,
title = "The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data",
abstract = "The balance of ribosomal proteins is important for the assembly of ribosomal subunits and cell viability. The synthesis of ribosomal proteins in a eukaryotic cell is controlled by various mechanisms, including autoregulation, which so far has been revealed for only a few of these proteins. We applied the photoactivatable 4-thiouridine-enhanced cross-linking and immunoprecipitation assay to HEK293T cells overproducing FLAG-labeled human ribosomal protein eL29 (eL29FLAG) to determine which RNAs other than rRNA interact with eL29. We demonstrated that eL29FLAG was incorporated into 60S subunits, and that ribosomes with those containing eL29FLAG were competent in translation. Analysis of the next generation sequencing data obtained from a DNA library derived from RNA fragments with covalently attached eL29FLAG peptide residues showed that the protein was cross-linked to the mRNA of the eL29-coding gene, which turned out to be its only major RNA target. The eL29FLAG cross-linking sites were located in the 3′ part of the mRNA coding sequence (CDS). A specific helix that mimics the eL29 binding site on 28S rRNA was proposed as a site that is recognized by the protein upon its binding to the cognate mRNA. In addition, it was found that both eL29FLAG mRNA and eL29 mRNA, unlike those of other ribosomal proteins, were co-immunoprecipitated with eL29FLAG from the ribosome-depleted cell lysate, and recombinant eL29 inhibited the translation of the eL29 mRNA CDS transcript in a cell-free system. All this suggests that human eL29 regulates its own synthesis via a feedback mechanism by binding to the cognate mRNA, preventing its translation.",
keywords = "Feedback mechanism, HEK293T cell Transfection, Human ribosomal protein eL29, In cell RNA-Protein cross-linking, Protein binding to its own mRNA, Regulation of gene expression, NUCLEAR, TRANSLATION, IDENTIFICATION, BIOGENESIS, PATHWAY, GENES, S14, SITES, EXPRESSION, SUBUNIT",
author = "Babaylova, {Elena S.} and Kolobova, {Alena V.} and Gopanenko, {Alexander V.} and Tupikin, {Alexey E.} and Kabilov, {Marsel R.} and Malygin, {Alexey A.} and Karpova, {Galina G.}",
note = "Copyright {\textcopyright} 2020 Elsevier B.V. and Soci{\'e}t{\'e} Fran{\c c}aise de Biochimie et Biologie Mol{\'e}culaire (SFBBM). All rights reserved.",
year = "2020",
month = oct,
day = "1",
doi = "10.1016/j.biochi.2020.07.019",
language = "English",
volume = "177",
pages = "68--77",
journal = "Biochimie",
issn = "0300-9084",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - The human ribosomal protein eL29 binds in vivo to the cognate mRNA by interacting with its coding sequence, as revealed from in-cell cross-linking data

AU - Babaylova, Elena S.

AU - Kolobova, Alena V.

AU - Gopanenko, Alexander V.

AU - Tupikin, Alexey E.

AU - Kabilov, Marsel R.

AU - Malygin, Alexey A.

AU - Karpova, Galina G.

N1 - Copyright © 2020 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.

PY - 2020/10/1

Y1 - 2020/10/1

N2 - The balance of ribosomal proteins is important for the assembly of ribosomal subunits and cell viability. The synthesis of ribosomal proteins in a eukaryotic cell is controlled by various mechanisms, including autoregulation, which so far has been revealed for only a few of these proteins. We applied the photoactivatable 4-thiouridine-enhanced cross-linking and immunoprecipitation assay to HEK293T cells overproducing FLAG-labeled human ribosomal protein eL29 (eL29FLAG) to determine which RNAs other than rRNA interact with eL29. We demonstrated that eL29FLAG was incorporated into 60S subunits, and that ribosomes with those containing eL29FLAG were competent in translation. Analysis of the next generation sequencing data obtained from a DNA library derived from RNA fragments with covalently attached eL29FLAG peptide residues showed that the protein was cross-linked to the mRNA of the eL29-coding gene, which turned out to be its only major RNA target. The eL29FLAG cross-linking sites were located in the 3′ part of the mRNA coding sequence (CDS). A specific helix that mimics the eL29 binding site on 28S rRNA was proposed as a site that is recognized by the protein upon its binding to the cognate mRNA. In addition, it was found that both eL29FLAG mRNA and eL29 mRNA, unlike those of other ribosomal proteins, were co-immunoprecipitated with eL29FLAG from the ribosome-depleted cell lysate, and recombinant eL29 inhibited the translation of the eL29 mRNA CDS transcript in a cell-free system. All this suggests that human eL29 regulates its own synthesis via a feedback mechanism by binding to the cognate mRNA, preventing its translation.

AB - The balance of ribosomal proteins is important for the assembly of ribosomal subunits and cell viability. The synthesis of ribosomal proteins in a eukaryotic cell is controlled by various mechanisms, including autoregulation, which so far has been revealed for only a few of these proteins. We applied the photoactivatable 4-thiouridine-enhanced cross-linking and immunoprecipitation assay to HEK293T cells overproducing FLAG-labeled human ribosomal protein eL29 (eL29FLAG) to determine which RNAs other than rRNA interact with eL29. We demonstrated that eL29FLAG was incorporated into 60S subunits, and that ribosomes with those containing eL29FLAG were competent in translation. Analysis of the next generation sequencing data obtained from a DNA library derived from RNA fragments with covalently attached eL29FLAG peptide residues showed that the protein was cross-linked to the mRNA of the eL29-coding gene, which turned out to be its only major RNA target. The eL29FLAG cross-linking sites were located in the 3′ part of the mRNA coding sequence (CDS). A specific helix that mimics the eL29 binding site on 28S rRNA was proposed as a site that is recognized by the protein upon its binding to the cognate mRNA. In addition, it was found that both eL29FLAG mRNA and eL29 mRNA, unlike those of other ribosomal proteins, were co-immunoprecipitated with eL29FLAG from the ribosome-depleted cell lysate, and recombinant eL29 inhibited the translation of the eL29 mRNA CDS transcript in a cell-free system. All this suggests that human eL29 regulates its own synthesis via a feedback mechanism by binding to the cognate mRNA, preventing its translation.

KW - Feedback mechanism

KW - HEK293T cell Transfection

KW - Human ribosomal protein eL29

KW - In cell RNA-Protein cross-linking

KW - Protein binding to its own mRNA

KW - Regulation of gene expression

KW - NUCLEAR

KW - TRANSLATION

KW - IDENTIFICATION

KW - BIOGENESIS

KW - PATHWAY

KW - GENES

KW - S14

KW - SITES

KW - EXPRESSION

KW - SUBUNIT

UR - http://www.scopus.com/inward/record.url?scp=85089797847&partnerID=8YFLogxK

U2 - 10.1016/j.biochi.2020.07.019

DO - 10.1016/j.biochi.2020.07.019

M3 - Article

C2 - 32798643

AN - SCOPUS:85089797847

VL - 177

SP - 68

EP - 77

JO - Biochimie

JF - Biochimie

SN - 0300-9084

ER -

ID: 25302522