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Far upstream element-binding protein 1 and RNA secondary structure both mediate second-step splicing repression.

Splicing of mRNA precursors consists of two steps that are almost invariably tightly coupled to facilitate efficient generation of spliced mRNA. However, we described previously a splicing substrate that is completely blocked after the first step. We have now investigated the basis for this unusual... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America July 16, 2013, Vol.110(29), pp.E2687-E2695
Main Author: Li, Huang
Other Authors: Wang, Zhijia , Zhou, Xuexia , Cheng, Yuanming , Xie, Zhiqin , Manley, James L , Feng, Ying
Format: Electronic Article Electronic Article
Language: English
Subjects:
RNA
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1310607110
Link: http://search.proquest.com/docview/1401091463/?pq-origsite=primo
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title: Far upstream element-binding protein 1 and RNA secondary structure both mediate second-step splicing repression.
format: Article
creator:
  • Li, Huang
  • Wang, Zhijia
  • Zhou, Xuexia
  • Cheng, Yuanming
  • Xie, Zhiqin
  • Manley, James L
  • Feng, Ying
subjects:
  • Base Sequence–Genetics
  • Binding Sites–Genetics
  • Blotting, Western–Metabolism
  • DNA Helicases–Genetics
  • DNA Primers–Genetics
  • DNA-Binding Proteins–Metabolism
  • Electrophoretic Mobility Shift Assay–Genetics
  • Exons–Physiology
  • Gene Expression Regulation–Chemistry
  • Hela Cells–Metabolism
  • Humans–Physiology
  • Molecular Sequence Data–Physiology
  • Nucleic Acid Conformation–Physiology
  • RNA–Physiology
  • RNA Interference–Physiology
  • RNA Splicing–Physiology
  • Reverse Transcriptase Polymerase Chain Reaction–Physiology
  • DNA Primers
  • DNA-Binding Proteins
  • Fubp1 Protein, Human
  • RNA
  • DNA Helicases
ispartof: Proceedings of the National Academy of Sciences of the United States of America, July 16, 2013, Vol.110(29), pp.E2687-E2695
description: Splicing of mRNA precursors consists of two steps that are almost invariably tightly coupled to facilitate efficient generation of spliced mRNA. However, we described previously a splicing substrate that is completely blocked after the first step. We have now investigated the basis for this unusual second-step inhibition and unexpectedly elucidated two independent mechanisms. One involves a stem-loop structure located downstream of the 3'splice site, and the other involves an exonic splicing silencer (ESS) situated 3' to the structure. Both elements contribute to the second-step block in vitro and also cause exon skipping in vivo. Importantly, we identified far upstream element-binding protein 1 (FUBP1), a single-stranded DNA- and RNA-binding protein not previously implicated in splicing, as a strong ESS binding protein, and several assays implicate it in ESS function. We demonstrate using depletion/add-back experiments that FUBP1 acts as a second-step repressor in vitro and show by siRNA-mediated knockdown and overexpression assays that it modulates exon inclusion in vivo. Together, our results provide additional insights into splicing control, and identify FUBP1 as a splicing regulator.
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1310607110
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleFar upstream element-binding protein 1 and RNA secondary structure both mediate second-step splicing repression.
creatorLi, Huang ; Wang, Zhijia ; Zhou, Xuexia ; Cheng, Yuanming ; Xie, Zhiqin ; Manley, James L ; Feng, Ying
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identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1310607110
subjectBase Sequence–Genetics ; Binding Sites–Genetics ; Blotting, Western–Metabolism ; DNA Helicases–Genetics ; DNA Primers–Genetics ; DNA-Binding Proteins–Metabolism ; Electrophoretic Mobility Shift Assay–Genetics ; Exons–Physiology ; Gene Expression Regulation–Chemistry ; Hela Cells–Metabolism ; Humans–Physiology ; Molecular Sequence Data–Physiology ; Nucleic Acid Conformation–Physiology ; RNA–Physiology ; RNA Interference–Physiology ; RNA Splicing–Physiology ; Reverse Transcriptase Polymerase Chain Reaction–Physiology ; DNA Primers ; DNA-Binding Proteins ; Fubp1 Protein, Human ; RNA ; DNA Helicases
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descriptionSplicing of mRNA precursors consists of two steps that are almost invariably tightly coupled to facilitate efficient generation of spliced mRNA. However, we described previously a splicing substrate that is completely blocked after the first step. We have now investigated the basis for this unusual second-step inhibition and unexpectedly elucidated two independent mechanisms. One involves a stem-loop structure located downstream of the 3'splice site, and the other involves an exonic splicing silencer (ESS) situated 3' to the structure. Both elements contribute to the second-step block in vitro and also cause exon skipping in vivo. Importantly, we identified far upstream element-binding protein 1 (FUBP1), a single-stranded DNA- and RNA-binding protein not previously implicated in splicing, as a strong ESS binding protein, and several assays implicate it in ESS function. We demonstrate using depletion/add-back experiments that FUBP1 acts as a second-step repressor in vitro and show by siRNA-mediated knockdown and overexpression assays that it modulates exon inclusion in vivo. Together, our results provide additional insights into splicing control, and identify FUBP1 as a splicing regulator.
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authorLi, Huang ; Wang, Zhijia ; Zhou, Xuexia ; Cheng, Yuanming ; Xie, Zhiqin ; Manley, James L ; Feng, Ying
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