Contribution of Individual Amino Acids to the 5S RNA Binding Activity of the Xenopus Zinc Finger Protein p43.
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| Title: | Contribution of Individual Amino Acids to the 5S RNA Binding Activity of the Xenopus Zinc Finger Protein p43. |
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| Authors: | Simran S. Bhatia1, Tristen C. Weiss1, Paul J. Romaniuk1 pjr@uvic.ca |
| Source: | Biochemistry. 8/12/2008, Vol. 47 Issue 32, p8398-8405. 8p. 2 Diagrams, 2 Charts, 3 Graphs. |
| Subjects: | Xenopus, Zinc, Nucleoproteins, RNA, Amino acids |
| Abstract: | Xenopus zinc finger protein p43 binds to 5S RNA in immature oocytes to form a 42S ribonucleoprotein storage particle. To determine the role of individual zinc fingers of the protein in this RNA binding activity, a series of deletion and substitution mutants of p43 were constructed. The effects of the various mutations on the RNA binding activity of p43 were determined using a quantitative equilibrium binding assay. The results indicate that zinc fingers 1 and 4 of p43 are essential for the binding of the protein to 5S RNA. In the case of finger 1, four amino acids key to RNA binding are found on the same face of the α-helix, while in the case of finger 4, two key residues are clustered at the start of the α-helix. The similarities and differences in the mechanisms by which fingers 1 and 4 of p43 interact with 5S RNA are compared to the interaction of the zinc fingers of Xenopus transcription factor IIIA with 5S RNA. [ABSTRACT FROM AUTHOR] |
| Copyright of Biochemistry is the property of American Chemical Society 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: 34010827 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Contribution of Individual Amino Acids to the 5S RNA Binding Activity of the Xenopus Zinc Finger Protein p43. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Simran+S%2E+Bhatia%22">Simran S. Bhatia</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Tristen+C%2E+Weiss%22">Tristen C. Weiss</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Paul+J%2E+Romaniuk%22">Paul J. Romaniuk</searchLink><relatesTo>1</relatesTo><i> pjr@uvic.ca</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biochemistry%22">Biochemistry</searchLink>. 8/12/2008, Vol. 47 Issue 32, p8398-8405. 8p. 2 Diagrams, 2 Charts, 3 Graphs. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Xenopus%22">Xenopus</searchLink><br /><searchLink fieldCode="DE" term="%22Zinc%22">Zinc</searchLink><br /><searchLink fieldCode="DE" term="%22Nucleoproteins%22">Nucleoproteins</searchLink><br /><searchLink fieldCode="DE" term="%22RNA%22">RNA</searchLink><br /><searchLink fieldCode="DE" term="%22Amino+acids%22">Amino acids</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Xenopus zinc finger protein p43 binds to 5S RNA in immature oocytes to form a 42S ribonucleoprotein storage particle. To determine the role of individual zinc fingers of the protein in this RNA binding activity, a series of deletion and substitution mutants of p43 were constructed. The effects of the various mutations on the RNA binding activity of p43 were determined using a quantitative equilibrium binding assay. The results indicate that zinc fingers 1 and 4 of p43 are essential for the binding of the protein to 5S RNA. In the case of finger 1, four amino acids key to RNA binding are found on the same face of the α-helix, while in the case of finger 4, two key residues are clustered at the start of the α-helix. The similarities and differences in the mechanisms by which fingers 1 and 4 of p43 interact with 5S RNA are compared to the interaction of the zinc fingers of Xenopus transcription factor IIIA with 5S RNA. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biochemistry is the property of American Chemical Society 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: 10.1021/bi800080c Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 8398 Subjects: – SubjectFull: Xenopus Type: general – SubjectFull: Zinc Type: general – SubjectFull: Nucleoproteins Type: general – SubjectFull: RNA Type: general – SubjectFull: Amino acids Type: general Titles: – TitleFull: Contribution of Individual Amino Acids to the 5S RNA Binding Activity of the Xenopus Zinc Finger Protein p43. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Simran S. Bhatia – PersonEntity: Name: NameFull: Tristen C. Weiss – PersonEntity: Name: NameFull: Paul J. Romaniuk IsPartOfRelationships: – BibEntity: Dates: – D: 12 M: 08 Text: 8/12/2008 Type: published Y: 2008 Identifiers: – Type: issn-print Value: 00062960 Numbering: – Type: volume Value: 47 – Type: issue Value: 32 Titles: – TitleFull: Biochemistry Type: main |
| ResultId | 1 |