Biochemical and NMR Study on the Competition between Proteins 5C35, SRp4O, and Heterogeneous Nuclear Ribonucleoprotein Al at the HIV-l Tat Exon 2 Splicing Site*.
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| Title: | Biochemical and NMR Study on the Competition between Proteins 5C35, SRp4O, and Heterogeneous Nuclear Ribonucleoprotein Al at the HIV-l Tat Exon 2 Splicing Site*. |
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| Authors: | Hallay, Houda1, Locker, Nicolas2, Ayadi, Lilia1, Ropers, Deiphine1, Guittet, Eric2, Branlant, Christiane1 christiane.branlant@maem.uhp-nancy.fr |
| Source: | Journal of Biological Chemistry. 12/1/2006, Vol. 281 Issue 48, p37159-37174. 16p. 1 Diagram, 10 Graphs. |
| Subjects: | Biochemistry, Nuclear magnetic resonance, Proteins, Nucleoproteins, HIV, Apoptosis |
| Abstract: | The human immunodeficiency virus, type 1, Tat protein plays a key role in virus multiplication. Because of its apoptotic property, its production is highly controlled. It depends upon the A3 splicing site utilization. A key control of site A3 activity is the ESS2 splicing silencer, which is located within the long stem-loop structure 3 (SLS3), far downstream from site A3. Here, by enzymatic footprints, we demonstrate the presence of several heterogeneous nuclear ribonucleoprotein (hnRNP) A1-binding sites on SLS3 and show the importance of the C-terminal Gly domain of hnRNP A1 in the formation of stable complexes containing several hnRNP Al molecules bound on SLS3. Mutations in each of the UAG triplets in ESS2 strongly reduce the overall hnRNP A1 binding, showing the central role of ESS2 in hnRNP A1 assembly on SLS2-SLS3. Using NMR spectroscopy, we demonstrate the direct interaction of ESS2 with the RNA recognition motifs domains of hnRNP A1. This interaction has limited effect on the RNA two-dimensional structure. The SR proteins SC35 and SRp40 were found previously to be strong activators of site A3 utilization. By enzymatic and chemical footprints, we delineate their respective binding sites on SLS2 and SLS3 and find a strong similarity between the hnRNP A1-, SC35-, and SRp40-binding sites. The strongest SC35-binding site only has a modest contribution to site A3 activation. Hence, the main role of SR proteins at site A3 is to counteract hnRNP A1 binding on ESS2 and ESE2. Indeed, we found that ESE2 has inhibitory properties because of its ability to bind hnRNP A1. [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: 23576164 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Biochemical and NMR Study on the Competition between Proteins 5C35, SRp4O, and Heterogeneous Nuclear Ribonucleoprotein Al at the HIV-l Tat Exon 2 Splicing Site*. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Hallay%2C+Houda%22">Hallay, Houda</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Locker%2C+Nicolas%22">Locker, Nicolas</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Ayadi%2C+Lilia%22">Ayadi, Lilia</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Ropers%2C+Deiphine%22">Ropers, Deiphine</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Guittet%2C+Eric%22">Guittet, Eric</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Branlant%2C+Christiane%22">Branlant, Christiane</searchLink><relatesTo>1</relatesTo><i> christiane.branlant@maem.uhp-nancy.fr</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 12/1/2006, Vol. 281 Issue 48, p37159-37174. 16p. 1 Diagram, 10 Graphs. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Biochemistry%22">Biochemistry</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+magnetic+resonance%22">Nuclear magnetic resonance</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Nucleoproteins%22">Nucleoproteins</searchLink><br /><searchLink fieldCode="DE" term="%22HIV%22">HIV</searchLink><br /><searchLink fieldCode="DE" term="%22Apoptosis%22">Apoptosis</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The human immunodeficiency virus, type 1, Tat protein plays a key role in virus multiplication. Because of its apoptotic property, its production is highly controlled. It depends upon the A3 splicing site utilization. A key control of site A3 activity is the ESS2 splicing silencer, which is located within the long stem-loop structure 3 (SLS3), far downstream from site A3. Here, by enzymatic footprints, we demonstrate the presence of several heterogeneous nuclear ribonucleoprotein (hnRNP) A1-binding sites on SLS3 and show the importance of the C-terminal Gly domain of hnRNP A1 in the formation of stable complexes containing several hnRNP Al molecules bound on SLS3. Mutations in each of the UAG triplets in ESS2 strongly reduce the overall hnRNP A1 binding, showing the central role of ESS2 in hnRNP A1 assembly on SLS2-SLS3. Using NMR spectroscopy, we demonstrate the direct interaction of ESS2 with the RNA recognition motifs domains of hnRNP A1. This interaction has limited effect on the RNA two-dimensional structure. The SR proteins SC35 and SRp40 were found previously to be strong activators of site A3 utilization. By enzymatic and chemical footprints, we delineate their respective binding sites on SLS2 and SLS3 and find a strong similarity between the hnRNP A1-, SC35-, and SRp40-binding sites. The strongest SC35-binding site only has a modest contribution to site A3 activation. Hence, the main role of SR proteins at site A3 is to counteract hnRNP A1 binding on ESS2 and ESE2. Indeed, we found that ESE2 has inhibitory properties because of its ability to bind hnRNP A1. [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.M603864200 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 16 StartPage: 37159 Subjects: – SubjectFull: Biochemistry Type: general – SubjectFull: Nuclear magnetic resonance Type: general – SubjectFull: Proteins Type: general – SubjectFull: Nucleoproteins Type: general – SubjectFull: HIV Type: general – SubjectFull: Apoptosis Type: general Titles: – TitleFull: Biochemical and NMR Study on the Competition between Proteins 5C35, SRp4O, and Heterogeneous Nuclear Ribonucleoprotein Al at the HIV-l Tat Exon 2 Splicing Site*. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Hallay, Houda – PersonEntity: Name: NameFull: Locker, Nicolas – PersonEntity: Name: NameFull: Ayadi, Lilia – PersonEntity: Name: NameFull: Ropers, Deiphine – PersonEntity: Name: NameFull: Guittet, Eric – PersonEntity: Name: NameFull: Branlant, Christiane IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 12 Text: 12/1/2006 Type: published Y: 2006 Identifiers: – Type: issn-print Value: 00219258 Numbering: – Type: volume Value: 281 – Type: issue Value: 48 Titles: – TitleFull: Journal of Biological Chemistry Type: main |
| ResultId | 1 |
