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Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA. / Gopanenko, Alexander V.; Malygin, Alexey A.; Tupikin, Alexey E. et al.

In: Nucleic Acids Research, Vol. 45, No. 15, 06.09.2017, p. 9121-9137.

Research output: Contribution to journalArticlepeer-review

Harvard

Gopanenko, AV, Malygin, AA, Tupikin, AE, Laktionov, PP, Kabilov, MR & Karpova, GG 2017, 'Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA', Nucleic Acids Research, vol. 45, no. 15, pp. 9121-9137. https://doi.org/10.1093/nar/gkx559

APA

Gopanenko, A. V., Malygin, A. A., Tupikin, A. E., Laktionov, P. P., Kabilov, M. R., & Karpova, G. G. (2017). Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA. Nucleic Acids Research, 45(15), 9121-9137. https://doi.org/10.1093/nar/gkx559

Vancouver

Gopanenko AV, Malygin AA, Tupikin AE, Laktionov PP, Kabilov MR, Karpova GG. Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA. Nucleic Acids Research. 2017 Sept 6;45(15):9121-9137. doi: 10.1093/nar/gkx559

Author

Gopanenko, Alexander V. ; Malygin, Alexey A. ; Tupikin, Alexey E. et al. / Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA. In: Nucleic Acids Research. 2017 ; Vol. 45, No. 15. pp. 9121-9137.

BibTeX

@article{7d9ceb002d0f4fec9076c64748420bbb,
title = "Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA",
abstract = "Ribosomal proteins are involved in many cellular processes through interactions with various RNAs. Here, applying the photoactivatable-ribonucleosideenhanced cross-linking and immunoprecipitation approach to HEK293 cells overproducing ribosomal protein (rp) eS1, we determined the products of RNU5A-1 and RNU11 genes encoding U5 and U11 snRNAs as the RNA partners of ribosome-unbound rp eS1. U11 pre-snRNA-associated rp eS1 was revealed in the cytoplasm and nucleus where rp eS1- bound U11/U12 di-snRNP was also found. Utilizing recombinant rp eS1 and 4-thiouridine-containing U11 snRNA transcript, we identified an N-terminal peptide contacting the U-rich sequence in the Sm sitecontaining RNA region. We also showed that the rp eS1 binding site on U11 snRNA is located in the cleft between stem-loops I and III and that its structure mimics the respective site on the 18S rRNA. It was found that cell depletion of rp eS1 leads to a decrease in the splicing efficiency of minor introns and to an increase in the level of U11 pre-snRNA with the unprocessed 3″ terminus. Our findings demonstrate the engagement of human rp eS1 in events related to the U11 snRNA processing and to minor-class splicing. Contacts of rp eS1 with U5 snRNA in the minor precatalytic spliceosome are discussed.",
keywords = "Amino Acid Sequence, Base Sequence, Escherichia coli/genetics, HEK293 Cells, Humans, Introns, Models, Molecular, Nucleic Acid Conformation, Protein Biosynthesis, Protein Conformation, alpha-Helical, Protein Interaction Domains and Motifs, RNA Splicing, RNA, Ribosomal, 18S/genetics, RNA, Small Nuclear/chemistry, Ribonucleoproteins, Small Nuclear/genetics, Ribosomal Proteins/chemistry, Ribosomes/genetics, Spliceosomes/genetics, Thiouridine/metabolism, ENTRY SITE, PRE-MESSENGER-RNA, INTERACTS, 5 SPLICE-SITE, 40S RIBOSOME, 80S RIBOSOME, MECHANISM, BINDING, EXPRESSION, INSIGHTS",
author = "Gopanenko, {Alexander V.} and Malygin, {Alexey A.} and Tupikin, {Alexey E.} and Laktionov, {Pavel P.} and Kabilov, {Marsel R.} and Karpova, {Galina G.}",
note = "{\textcopyright} The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.",
year = "2017",
month = sep,
day = "6",
doi = "10.1093/nar/gkx559",
language = "English",
volume = "45",
pages = "9121--9137",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "15",

}

RIS

TY - JOUR

T1 - Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA

AU - Gopanenko, Alexander V.

AU - Malygin, Alexey A.

AU - Tupikin, Alexey E.

AU - Laktionov, Pavel P.

AU - Kabilov, Marsel R.

AU - Karpova, Galina G.

N1 - © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

PY - 2017/9/6

Y1 - 2017/9/6

N2 - Ribosomal proteins are involved in many cellular processes through interactions with various RNAs. Here, applying the photoactivatable-ribonucleosideenhanced cross-linking and immunoprecipitation approach to HEK293 cells overproducing ribosomal protein (rp) eS1, we determined the products of RNU5A-1 and RNU11 genes encoding U5 and U11 snRNAs as the RNA partners of ribosome-unbound rp eS1. U11 pre-snRNA-associated rp eS1 was revealed in the cytoplasm and nucleus where rp eS1- bound U11/U12 di-snRNP was also found. Utilizing recombinant rp eS1 and 4-thiouridine-containing U11 snRNA transcript, we identified an N-terminal peptide contacting the U-rich sequence in the Sm sitecontaining RNA region. We also showed that the rp eS1 binding site on U11 snRNA is located in the cleft between stem-loops I and III and that its structure mimics the respective site on the 18S rRNA. It was found that cell depletion of rp eS1 leads to a decrease in the splicing efficiency of minor introns and to an increase in the level of U11 pre-snRNA with the unprocessed 3″ terminus. Our findings demonstrate the engagement of human rp eS1 in events related to the U11 snRNA processing and to minor-class splicing. Contacts of rp eS1 with U5 snRNA in the minor precatalytic spliceosome are discussed.

AB - Ribosomal proteins are involved in many cellular processes through interactions with various RNAs. Here, applying the photoactivatable-ribonucleosideenhanced cross-linking and immunoprecipitation approach to HEK293 cells overproducing ribosomal protein (rp) eS1, we determined the products of RNU5A-1 and RNU11 genes encoding U5 and U11 snRNAs as the RNA partners of ribosome-unbound rp eS1. U11 pre-snRNA-associated rp eS1 was revealed in the cytoplasm and nucleus where rp eS1- bound U11/U12 di-snRNP was also found. Utilizing recombinant rp eS1 and 4-thiouridine-containing U11 snRNA transcript, we identified an N-terminal peptide contacting the U-rich sequence in the Sm sitecontaining RNA region. We also showed that the rp eS1 binding site on U11 snRNA is located in the cleft between stem-loops I and III and that its structure mimics the respective site on the 18S rRNA. It was found that cell depletion of rp eS1 leads to a decrease in the splicing efficiency of minor introns and to an increase in the level of U11 pre-snRNA with the unprocessed 3″ terminus. Our findings demonstrate the engagement of human rp eS1 in events related to the U11 snRNA processing and to minor-class splicing. Contacts of rp eS1 with U5 snRNA in the minor precatalytic spliceosome are discussed.

KW - Amino Acid Sequence

KW - Base Sequence

KW - Escherichia coli/genetics

KW - HEK293 Cells

KW - Humans

KW - Introns

KW - Models, Molecular

KW - Nucleic Acid Conformation

KW - Protein Biosynthesis

KW - Protein Conformation, alpha-Helical

KW - Protein Interaction Domains and Motifs

KW - RNA Splicing

KW - RNA, Ribosomal, 18S/genetics

KW - RNA, Small Nuclear/chemistry

KW - Ribonucleoproteins, Small Nuclear/genetics

KW - Ribosomal Proteins/chemistry

KW - Ribosomes/genetics

KW - Spliceosomes/genetics

KW - Thiouridine/metabolism

KW - ENTRY SITE

KW - PRE-MESSENGER-RNA

KW - INTERACTS

KW - 5 SPLICE-SITE

KW - 40S RIBOSOME

KW - 80S RIBOSOME

KW - MECHANISM

KW - BINDING

KW - EXPRESSION

KW - INSIGHTS

UR - http://www.scopus.com/inward/record.url?scp=85031048737&partnerID=8YFLogxK

U2 - 10.1093/nar/gkx559

DO - 10.1093/nar/gkx559

M3 - Article

C2 - 28666385

AN - SCOPUS:85031048737

VL - 45

SP - 9121

EP - 9137

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 15

ER -

ID: 9893634