The RNA Binding Motif Protein 15B (RBM1 B/OTT3) Is a Functional Competitor of Serine-Arginine (SR) Proteins and Antagonizes the Positive Effect of the CDK11p110 -Cyclin L2α Complex on Splicing.
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| Title: | The RNA Binding Motif Protein 15B (RBM1 B/OTT3) Is a Functional Competitor of Serine-Arginine (SR) Proteins and Antagonizes the Positive Effect of the CDK11p110 -Cyclin L2α Complex on Splicing. |
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| Authors: | Loyer, Pascal1,2, Busson, Adeline1, Trembley, Janeen H.2, Hyle, Judith2, Grenet, Jose2, Wei Zhao3, Ribault, Catherine1, Montier, Tristan4, Kidd, Vincent J.2, Lahti, Jill M.2 Jill.Lahti@stjude.org |
| Source: | Journal of Biological Chemistry. 1/7/2011, Vol. 286 Issue 1, p147-159. 13p. |
| Subjects: | Protein binding, RNA splicing, Molecular genetics, Epstein-Barr virus, Messenger RNA, Serine proteinases, Arginine |
| Abstract: | Here, we report the identification of the RNA binding motif protein RBM15B/OTT3 as a new CDK11p110 binding partner that alters the effects of CDK11 on splicing. RBM15B was initially identified as a binding partner of the Epstein-Barr virus mRNA export factor and, more recently, as a cofactor of the nuclear export receptor NXF1. In this study, we found that RBM15B co-elutes with CDK11p110, cyclin L2α, and serine-arginine (SR) proteins, including SF2/ASF, in a large nuclear complex of ~1-MDa molecular mass following size exclusion chromatography. Using co-immunoprecipitation experiments and in vitro pulldown assays, we mapped two distinct domains of RBM15B that are essential for its direct interaction with the N-terminal extension of CDK11p110, cyclin L2α, and SR proteins such as 9G8 and SF2/ASF. Finally, we established that RBM15B is a functional competitor of the SR proteins SF2/ASF and 9G8, inhibits formation of the functional spliceosomal E complex, and antagonizes the positive effect of the CDK11p110-cyclin L2α complex on splicing both in vitro and in vivo. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 63018263 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: The RNA Binding Motif Protein 15B (RBM1 B/OTT3) Is a Functional Competitor of Serine-Arginine (SR) Proteins and Antagonizes the Positive Effect of the CDK11<superscript>p110</superscript> -Cyclin L2α Complex on Splicing. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Loyer%2C+Pascal%22">Loyer, Pascal</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Busson%2C+Adeline%22">Busson, Adeline</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Trembley%2C+Janeen+H%2E%22">Trembley, Janeen H.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Hyle%2C+Judith%22">Hyle, Judith</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Grenet%2C+Jose%22">Grenet, Jose</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Wei+Zhao%22">Wei Zhao</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Ribault%2C+Catherine%22">Ribault, Catherine</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Montier%2C+Tristan%22">Montier, Tristan</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Kidd%2C+Vincent+J%2E%22">Kidd, Vincent J.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Lahti%2C+Jill+M%2E%22">Lahti, Jill M.</searchLink><relatesTo>2</relatesTo><i> Jill.Lahti@stjude.org</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 1/7/2011, Vol. 286 Issue 1, p147-159. 13p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Protein+binding%22">Protein binding</searchLink><br /><searchLink fieldCode="DE" term="%22RNA+splicing%22">RNA splicing</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+genetics%22">Molecular genetics</searchLink><br /><searchLink fieldCode="DE" term="%22Epstein-Barr+virus%22">Epstein-Barr virus</searchLink><br /><searchLink fieldCode="DE" term="%22Messenger+RNA%22">Messenger RNA</searchLink><br /><searchLink fieldCode="DE" term="%22Serine+proteinases%22">Serine proteinases</searchLink><br /><searchLink fieldCode="DE" term="%22Arginine%22">Arginine</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Here, we report the identification of the RNA binding motif protein RBM15B/OTT3 as a new CDK11p110 binding partner that alters the effects of CDK11 on splicing. RBM15B was initially identified as a binding partner of the Epstein-Barr virus mRNA export factor and, more recently, as a cofactor of the nuclear export receptor NXF1. In this study, we found that RBM15B co-elutes with CDK11p110, cyclin L2α, and serine-arginine (SR) proteins, including SF2/ASF, in a large nuclear complex of ~1-MDa molecular mass following size exclusion chromatography. Using co-immunoprecipitation experiments and in vitro pulldown assays, we mapped two distinct domains of RBM15B that are essential for its direct interaction with the N-terminal extension of CDK11p110, cyclin L2α, and SR proteins such as 9G8 and SF2/ASF. Finally, we established that RBM15B is a functional competitor of the SR proteins SF2/ASF and 9G8, inhibits formation of the functional spliceosomal E complex, and antagonizes the positive effect of the CDK11p110-cyclin L2α complex on splicing both in vitro and in vivo. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1074/jbc.M110.192518 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 13 StartPage: 147 Subjects: – SubjectFull: Protein binding Type: general – SubjectFull: RNA splicing Type: general – SubjectFull: Molecular genetics Type: general – SubjectFull: Epstein-Barr virus Type: general – SubjectFull: Messenger RNA Type: general – SubjectFull: Serine proteinases Type: general – SubjectFull: Arginine Type: general Titles: – TitleFull: The RNA Binding Motif Protein 15B (RBM1 B/OTT3) Is a Functional Competitor of Serine-Arginine (SR) Proteins and Antagonizes the Positive Effect of the CDK11p110 -Cyclin L2α Complex on Splicing. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Loyer, Pascal – PersonEntity: Name: NameFull: Busson, Adeline – PersonEntity: Name: NameFull: Trembley, Janeen H. – PersonEntity: Name: NameFull: Hyle, Judith – PersonEntity: Name: NameFull: Grenet, Jose – PersonEntity: Name: NameFull: Wei Zhao – PersonEntity: Name: NameFull: Ribault, Catherine – PersonEntity: Name: NameFull: Montier, Tristan – PersonEntity: Name: NameFull: Kidd, Vincent J. – PersonEntity: Name: NameFull: Lahti, Jill M. IsPartOfRelationships: – BibEntity: Dates: – D: 07 M: 01 Text: 1/7/2011 Type: published Y: 2011 Identifiers: – Type: issn-print Value: 00219258 Numbering: – Type: volume Value: 286 – Type: issue Value: 1 Titles: – TitleFull: Journal of Biological Chemistry Type: main |
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