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RNA-binding protein Rbpms is represented in human retinas by isoforms A and C and its transcriptional regulation involves Sp1-binding site

Rbpms (RNA-binding protein with multiple splicing) is a member of the RRM (RNA Recognition Motif) family of RNA-binding proteins, which is expressed as multiple alternatively spliced transcripts encoding different protein isoforms. We have shown earlier that Rbpms expression in the retina is restric... Full description

Journal Title: Molecular genetics and genomics : MGG 2018-02-08, Vol.293 (4), p.819-830
Main Author: Ye, Linda
Other Authors: Gu, Lei , Caprioli, Joseph , Piri, Natik
Format: Electronic Article Electronic Article
Language: English
Subjects:
RNA
Publisher: Berlin/Heidelberg: Springer Berlin Heidelberg
ID: ISSN: 1617-4615
Link: https://www.ncbi.nlm.nih.gov/pubmed/29423656
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title: RNA-binding protein Rbpms is represented in human retinas by isoforms A and C and its transcriptional regulation involves Sp1-binding site
format: Article
creator:
  • Ye, Linda
  • Gu, Lei
  • Caprioli, Joseph
  • Piri, Natik
subjects:
  • Activator protein 1
  • Alternative splicing
  • Animal Genetics and Genomics
  • Article
  • Binding sites
  • Biochemistry
  • Biomedical and Life Sciences
  • Computer applications
  • CpG islands
  • Exons
  • Eye Proteins - genetics
  • Eye Proteins - metabolism
  • Gene expression
  • Gene regulation
  • general
  • HEK293 Cells
  • Human Genetics
  • Humans
  • Isoforms
  • Life Sciences
  • Microbial Genetics and Genomics
  • Mutagenesis
  • Mutagenesis, Site-Directed
  • Mutation
  • NF-kappa B - genetics
  • NF-kappa B - metabolism
  • NF-κB protein
  • Oligonucleotides
  • Original Article
  • Plant Genetics and Genomics
  • Promoter
  • Protein Isoforms - biosynthesis
  • Protein Isoforms - genetics
  • Proteins
  • Response Elements - physiology
  • Retina
  • Retina - metabolism
  • Retinal ganglion cells
  • Ribonucleic acid
  • RNA
  • RNA-binding protein
  • RNA-Binding Proteins - biosynthesis
  • RNA-Binding Proteins - genetics
  • Site-directed mutagenesis
  • Sp1 protein
  • Sp1 Transcription Factor - genetics
  • Sp1 Transcription Factor - metabolism
  • Transcription activation
  • Transcription factors
  • Transcription, Genetic
ispartof: Molecular genetics and genomics : MGG, 2018-02-08, Vol.293 (4), p.819-830
description: Rbpms (RNA-binding protein with multiple splicing) is a member of the RRM (RNA Recognition Motif) family of RNA-binding proteins, which is expressed as multiple alternatively spliced transcripts encoding different protein isoforms. We have shown earlier that Rbpms expression in the retina is restricted to retinal ganglion cells (RGCs), and have characterized this gene as a marker for RGCs. The aim of this study was to identify isoforms representing Rbpms in human retinas and to analyze its transcriptional regulation. We found that Rbpms is expressed as transcription variants 1 and 3 encoding isoforms A and C, respectively. These isoforms are encoded by the same first 6 exons but have different C-terminal ends encoded by exon 8 in variant 1 and exon 7 in variant 3. Computational analysis of the Rbpms 5′ untranslated and flanking regions reveals the presence of three CpG islands and four predicted promoter regions (PPRs). The effect of PPR 1 (− 1672/− 1420) and PPR2 (− 330/− 79) on transcriptional activation was minimal, whereas PPR 3 (− 73/+ 177) and PPR4 (+ 274/+ 524) induced the expression by ~ 7 and ninefold compared to control, respectively. The maximum activity, a 30-fold increase above the control level, was obtained from the construct containing both PPRs 3 and 4. Site-directed mutagenesis of several cis -elements within PPR3 and PPR4 including five for Sp1, one for AP1, and two for NF-kB showed that mutation of the first three and especially the first GC box resulted in a threefold downregulation of gene expression. AP1, NF-kB, and two downstream Sp1 sites had no significant effect on expression level. The possible involvement of the GC box 1 at position − 54 in transcriptional regulation of Rbpms was corroborated by EMSA, which showed formation of a DNA–protein complex in the presence of the oligonucleotide corresponding to this Sp1-binding site.
language: eng
source:
identifier: ISSN: 1617-4615
fulltext: no_fulltext
issn:
  • 1617-4615
  • 1617-4623
url: Link


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titleRNA-binding protein Rbpms is represented in human retinas by isoforms A and C and its transcriptional regulation involves Sp1-binding site
creatorYe, Linda ; Gu, Lei ; Caprioli, Joseph ; Piri, Natik
creatorcontribYe, Linda ; Gu, Lei ; Caprioli, Joseph ; Piri, Natik
descriptionRbpms (RNA-binding protein with multiple splicing) is a member of the RRM (RNA Recognition Motif) family of RNA-binding proteins, which is expressed as multiple alternatively spliced transcripts encoding different protein isoforms. We have shown earlier that Rbpms expression in the retina is restricted to retinal ganglion cells (RGCs), and have characterized this gene as a marker for RGCs. The aim of this study was to identify isoforms representing Rbpms in human retinas and to analyze its transcriptional regulation. We found that Rbpms is expressed as transcription variants 1 and 3 encoding isoforms A and C, respectively. These isoforms are encoded by the same first 6 exons but have different C-terminal ends encoded by exon 8 in variant 1 and exon 7 in variant 3. Computational analysis of the Rbpms 5′ untranslated and flanking regions reveals the presence of three CpG islands and four predicted promoter regions (PPRs). The effect of PPR 1 (− 1672/− 1420) and PPR2 (− 330/− 79) on transcriptional activation was minimal, whereas PPR 3 (− 73/+ 177) and PPR4 (+ 274/+ 524) induced the expression by ~ 7 and ninefold compared to control, respectively. The maximum activity, a 30-fold increase above the control level, was obtained from the construct containing both PPRs 3 and 4. Site-directed mutagenesis of several cis -elements within PPR3 and PPR4 including five for Sp1, one for AP1, and two for NF-kB showed that mutation of the first three and especially the first GC box resulted in a threefold downregulation of gene expression. AP1, NF-kB, and two downstream Sp1 sites had no significant effect on expression level. The possible involvement of the GC box 1 at position − 54 in transcriptional regulation of Rbpms was corroborated by EMSA, which showed formation of a DNA–protein complex in the presence of the oligonucleotide corresponding to this Sp1-binding site.
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subjectActivator protein 1 ; Alternative splicing ; Animal Genetics and Genomics ; Article ; Binding sites ; Biochemistry ; Biomedical and Life Sciences ; Computer applications ; CpG islands ; Exons ; Eye Proteins - genetics ; Eye Proteins - metabolism ; Gene expression ; Gene regulation ; general ; HEK293 Cells ; Human Genetics ; Humans ; Isoforms ; Life Sciences ; Microbial Genetics and Genomics ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutation ; NF-kappa B - genetics ; NF-kappa B - metabolism ; NF-κB protein ; Oligonucleotides ; Original Article ; Plant Genetics and Genomics ; Promoter ; Protein Isoforms - biosynthesis ; Protein Isoforms - genetics ; Proteins ; Response Elements - physiology ; Retina ; Retina - metabolism ; Retinal ganglion cells ; Ribonucleic acid ; RNA ; RNA-binding protein ; RNA-Binding Proteins - biosynthesis ; RNA-Binding Proteins - genetics ; Site-directed mutagenesis ; Sp1 protein ; Sp1 Transcription Factor - genetics ; Sp1 Transcription Factor - metabolism ; Transcription activation ; Transcription factors ; Transcription, Genetic
ispartofMolecular genetics and genomics : MGG, 2018-02-08, Vol.293 (4), p.819-830
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descriptionRbpms (RNA-binding protein with multiple splicing) is a member of the RRM (RNA Recognition Motif) family of RNA-binding proteins, which is expressed as multiple alternatively spliced transcripts encoding different protein isoforms. We have shown earlier that Rbpms expression in the retina is restricted to retinal ganglion cells (RGCs), and have characterized this gene as a marker for RGCs. The aim of this study was to identify isoforms representing Rbpms in human retinas and to analyze its transcriptional regulation. We found that Rbpms is expressed as transcription variants 1 and 3 encoding isoforms A and C, respectively. These isoforms are encoded by the same first 6 exons but have different C-terminal ends encoded by exon 8 in variant 1 and exon 7 in variant 3. Computational analysis of the Rbpms 5′ untranslated and flanking regions reveals the presence of three CpG islands and four predicted promoter regions (PPRs). The effect of PPR 1 (− 1672/− 1420) and PPR2 (− 330/− 79) on transcriptional activation was minimal, whereas PPR 3 (− 73/+ 177) and PPR4 (+ 274/+ 524) induced the expression by ~ 7 and ninefold compared to control, respectively. The maximum activity, a 30-fold increase above the control level, was obtained from the construct containing both PPRs 3 and 4. Site-directed mutagenesis of several cis -elements within PPR3 and PPR4 including five for Sp1, one for AP1, and two for NF-kB showed that mutation of the first three and especially the first GC box resulted in a threefold downregulation of gene expression. AP1, NF-kB, and two downstream Sp1 sites had no significant effect on expression level. The possible involvement of the GC box 1 at position − 54 in transcriptional regulation of Rbpms was corroborated by EMSA, which showed formation of a DNA–protein complex in the presence of the oligonucleotide corresponding to this Sp1-binding site.
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0Activator protein 1
1Alternative splicing
2Animal Genetics and Genomics
3Article
4Binding sites
5Biochemistry
6Biomedical and Life Sciences
7Computer applications
8CpG islands
9Exons
10Eye Proteins - genetics
11Eye Proteins - metabolism
12Gene expression
13Gene regulation
14general
15HEK293 Cells
16Human Genetics
17Humans
18Isoforms
19Life Sciences
20Microbial Genetics and Genomics
21Mutagenesis
22Mutagenesis, Site-Directed
23Mutation
24NF-kappa B - genetics
25NF-kappa B - metabolism
26NF-κB protein
27Oligonucleotides
28Original Article
29Plant Genetics and Genomics
30Promoter
31Protein Isoforms - biosynthesis
32Protein Isoforms - genetics
33Proteins
34Response Elements - physiology
35Retina
36Retina - metabolism
37Retinal ganglion cells
38Ribonucleic acid
39RNA
40RNA-binding protein
41RNA-Binding Proteins - biosynthesis
42RNA-Binding Proteins - genetics
43Site-directed mutagenesis
44Sp1 protein
45Sp1 Transcription Factor - genetics
46Sp1 Transcription Factor - metabolism
47Transcription activation
48Transcription factors
49Transcription, Genetic
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42RNA-Binding Proteins - genetics
43Site-directed mutagenesis
44Sp1 protein
45Sp1 Transcription Factor - genetics
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atitleRNA-binding protein Rbpms is represented in human retinas by isoforms A and C and its transcriptional regulation involves Sp1-binding site
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abstractRbpms (RNA-binding protein with multiple splicing) is a member of the RRM (RNA Recognition Motif) family of RNA-binding proteins, which is expressed as multiple alternatively spliced transcripts encoding different protein isoforms. We have shown earlier that Rbpms expression in the retina is restricted to retinal ganglion cells (RGCs), and have characterized this gene as a marker for RGCs. The aim of this study was to identify isoforms representing Rbpms in human retinas and to analyze its transcriptional regulation. We found that Rbpms is expressed as transcription variants 1 and 3 encoding isoforms A and C, respectively. These isoforms are encoded by the same first 6 exons but have different C-terminal ends encoded by exon 8 in variant 1 and exon 7 in variant 3. Computational analysis of the Rbpms 5′ untranslated and flanking regions reveals the presence of three CpG islands and four predicted promoter regions (PPRs). The effect of PPR 1 (− 1672/− 1420) and PPR2 (− 330/− 79) on transcriptional activation was minimal, whereas PPR 3 (− 73/+ 177) and PPR4 (+ 274/+ 524) induced the expression by ~ 7 and ninefold compared to control, respectively. The maximum activity, a 30-fold increase above the control level, was obtained from the construct containing both PPRs 3 and 4. Site-directed mutagenesis of several cis -elements within PPR3 and PPR4 including five for Sp1, one for AP1, and two for NF-kB showed that mutation of the first three and especially the first GC box resulted in a threefold downregulation of gene expression. AP1, NF-kB, and two downstream Sp1 sites had no significant effect on expression level. The possible involvement of the GC box 1 at position − 54 in transcriptional regulation of Rbpms was corroborated by EMSA, which showed formation of a DNA–protein complex in the presence of the oligonucleotide corresponding to this Sp1-binding site.
copBerlin/Heidelberg
pubSpringer Berlin Heidelberg
pmid29423656
doi10.1007/s00438-018-1423-8
orcididhttps://orcid.org/0000-0002-0134-1996
oafree_for_read