Open Access
Nucleic Acids Research, volume 45, issue 15, pages 9121-9137
Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA
Gopanenko Alexander V
1, 2
,
Malygin Alexey A
1, 2
,
Tupikin Alexey E
3
,
Laktionov Pavel P.
3
,
Карпова Г. Г.
1, 2
Publication type: Journal Article
Publication date: 2017-06-28
Journal:
Nucleic Acids Research
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 14.9
ISSN: 03051048, 13624962
PubMed ID:
28666385
Genetics
Abstract
Abstract Ribosomal proteins are involved in many cellular processes through interactions with various RNAs. Here, applying the photoactivatable-ribonucleoside-enhanced 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 site-containing 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 pre-catalytic spliceosome are discussed.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Gopanenko A. V. et al. Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA // Nucleic Acids Research. 2017. Vol. 45. No. 15. pp. 9121-9137.
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Gopanenko A. V., Malygin A. A., Tupikin A. E., Laktionov P. P., Kabilov M. R., Карпова Г. Г. Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA // Nucleic Acids Research. 2017. Vol. 45. No. 15. pp. 9121-9137.
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TY - JOUR
DO - 10.1093/nar/gkx559
UR - https://doi.org/10.1093%2Fnar%2Fgkx559
TI - Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA
T2 - Nucleic Acids Research
AU - Malygin, Alexey A
AU - Laktionov, Pavel P.
AU - Gopanenko, Alexander V
AU - Tupikin, Alexey E
AU - Kabilov, Marsel R.
AU - Карпова, Г. Г.
PY - 2017
DA - 2017/06/28 00:00:00
PB - Oxford University Press
SP - 9121-9137
IS - 15
VL - 45
PMID - 28666385
SN - 0305-1048
SN - 1362-4962
ER -
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@article{2017_Gopanenko,
author = {Alexey A Malygin and Pavel P. Laktionov and Alexander V Gopanenko and Alexey E Tupikin and Marsel R. Kabilov and Г. Г. Карпова},
title = {Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA},
journal = {Nucleic Acids Research},
year = {2017},
volume = {45},
publisher = {Oxford University Press},
month = {jun},
url = {https://doi.org/10.1093%2Fnar%2Fgkx559},
number = {15},
pages = {9121--9137},
doi = {10.1093/nar/gkx559}
}
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Gopanenko, Alexander V., et al. “Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA.” Nucleic Acids Research, vol. 45, no. 15, Jun. 2017, pp. 9121-9137. https://doi.org/10.1093%2Fnar%2Fgkx559.
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