2j8p

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==Overview==
==Overview==
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Yeast Rna15 and its vertebrate orthologue CstF-64 play critical roles in, mRNA 3 '-end processing and in transcription termination downstream of, poly(A) sites. These proteins contain N-terminal domains that recognize, the poly(A) site, but little is known about their highly conserved, C-terminal regions. Here we show by NMR that the C-terminal domains of, CstF-64 and Rna15 fold into a three-helix bundle with an uncommon, topological arrangement. The structure defines a cluster of evolutionary, conserved yet exposed residues we show to be essential for the interaction, between Pcf11 and Rna15. Furthermore, we demonstrate that this interaction, is critical for the function of Rna15 in 3 '-end processing but, dispensable for transcription termination. The C-terminal domain of the, Rna15 homologue Pti1 contains critical sequence alterations within this, region that are predicted to prevent Pcf11 interaction, providing an, explanation for the distinct functions of these two closely related, proteins in the 3 '-end formation of RNA polymerase II transcripts. These, results define the role of the C-terminal half of Rna15 and provide, insight into the network of protein/protein interactions responsible for, assembly of the 3 '-end processing apparatus.
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Yeast Rna15 and its vertebrate orthologue CstF-64 play critical roles in mRNA 3 '-end processing and in transcription termination downstream of poly(A) sites. These proteins contain N-terminal domains that recognize the poly(A) site, but little is known about their highly conserved C-terminal regions. Here we show by NMR that the C-terminal domains of CstF-64 and Rna15 fold into a three-helix bundle with an uncommon topological arrangement. The structure defines a cluster of evolutionary conserved yet exposed residues we show to be essential for the interaction between Pcf11 and Rna15. Furthermore, we demonstrate that this interaction is critical for the function of Rna15 in 3 '-end processing but dispensable for transcription termination. The C-terminal domain of the Rna15 homologue Pti1 contains critical sequence alterations within this region that are predicted to prevent Pcf11 interaction, providing an explanation for the distinct functions of these two closely related proteins in the 3 '-end formation of RNA polymerase II transcripts. These results define the role of the C-terminal half of Rna15 and provide insight into the network of protein/protein interactions responsible for assembly of the 3 '-end processing apparatus.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Agrawal, S.]]
[[Category: Agrawal, S.]]
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[[Category: Baecke, J.De.]]
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[[Category: Baecke, J De.]]
[[Category: Cheng, H.]]
[[Category: Cheng, H.]]
[[Category: Moore, C.]]
[[Category: Moore, C.]]
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[[Category: Perez-Canadillas, J.M.]]
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[[Category: Perez-Canadillas, J M.]]
[[Category: Qu, X.]]
[[Category: Qu, X.]]
[[Category: Varani, G.]]
[[Category: Varani, G.]]
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[[Category: rna-binding]]
[[Category: rna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:37:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:31 2008''

Revision as of 16:00, 21 February 2008


2j8p

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NMR STRUCTURE OF C-TERMINAL DOMAIN OF HUMAN CSTF-64

Overview

Yeast Rna15 and its vertebrate orthologue CstF-64 play critical roles in mRNA 3 '-end processing and in transcription termination downstream of poly(A) sites. These proteins contain N-terminal domains that recognize the poly(A) site, but little is known about their highly conserved C-terminal regions. Here we show by NMR that the C-terminal domains of CstF-64 and Rna15 fold into a three-helix bundle with an uncommon topological arrangement. The structure defines a cluster of evolutionary conserved yet exposed residues we show to be essential for the interaction between Pcf11 and Rna15. Furthermore, we demonstrate that this interaction is critical for the function of Rna15 in 3 '-end processing but dispensable for transcription termination. The C-terminal domain of the Rna15 homologue Pti1 contains critical sequence alterations within this region that are predicted to prevent Pcf11 interaction, providing an explanation for the distinct functions of these two closely related proteins in the 3 '-end formation of RNA polymerase II transcripts. These results define the role of the C-terminal half of Rna15 and provide insight into the network of protein/protein interactions responsible for assembly of the 3 '-end processing apparatus.

About this Structure

2J8P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3'-end processing., Qu X, Perez-Canadillas JM, Agrawal S, De Baecke J, Cheng H, Varani G, Moore C, J Biol Chem. 2007 Jan 19;282(3):2101-15. Epub 2006 Nov 20. PMID:17116658

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