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  Retention and splicing complex (RES) - the importance of cooperativity.

Wysoczanski, P., & Zweckstetter, M. (2016). Retention and splicing complex (RES) - the importance of cooperativity. RNA Biology, 13(2), 128-133. doi:10.1080/15476286.2015.1096484.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-0A94-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-296C-D
Genre: Journal Article

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 Creators:
Wysoczanski, P.1, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              

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Free keywords: Cooperativity; NMR spectroscopy; Spliceosome; Structure
 Abstract: One of the great challenges to structural biologists lies in explaining the complexities of the spliceosome - a ribosome-sized molecular machine that is assembled in a step-wise manner and is responsible for pre-mRNA splicing. The spliceosome is both fascinating and difficult to work with, because of its dynamic nature. At each discrete step of splicing tens of proteins come and go orchestrating the functional transition through massive structural rearrangements. The retention and splicing complex (RES) is an important splicing factor interacting with pre-mRNA at the onset of the first transesterification reaction. RES is a specific splicing factor for a number of genes and is important for controlling pre-mRNA retention in the nucleus. RES is a 71kDa heterotrimer composed of the 3 proteins Pml1p, Bud13p and Snu17p. We solved the 3-dimensional structure of the core of the RES complex as well as the 2 dimers, Snu17p-Bud13p and Snu17p-Pml1p. Further biophysical analysis revealed an astounding cooperativity that governs the assembly of this trimeric complex as well as its interaction with pre-mRNA. The more than 100-fold cooperativity originates from the progressive rigidification of Snu17p upon coupled binding-and-folding of protein regions, which are disordered in the unbound state. Our work highlights the role of cooperativity in the spliceosome and poses new questions about the structure and assembly of the spliceosome.

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Language(s): eng - English
 Dates: 2015-10-192016
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1080/15476286.2015.1096484
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Title: RNA Biology
Source Genre: Journal
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Pages: - Volume / Issue: 13 (2) Sequence Number: - Start / End Page: 128 - 133 Identifier: -