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.
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.)
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  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.
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  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>
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  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.
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  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>
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  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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        Value: 10.1074/jbc.M110.192518
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      – Code: eng
        Text: English
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        PageCount: 13
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      – SubjectFull: Protein binding
        Type: general
      – SubjectFull: RNA splicing
        Type: general
      – SubjectFull: Molecular genetics
        Type: general
      – SubjectFull: Epstein-Barr virus
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      – SubjectFull: Messenger RNA
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      – SubjectFull: Serine proteinases
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      – SubjectFull: Arginine
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      – 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.
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              Text: 1/7/2011
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