English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Direct probing of RNA structure and RNA-protein interactions in purifies HeLa cells and yeast spliceosomal U4/U6.U5 tri-snRNP particles

Mougin, A., Gottschalk, A., Fabrizio, P., Luehrmann, R., & Branlant, C. (2002). Direct probing of RNA structure and RNA-protein interactions in purifies HeLa cells and yeast spliceosomal U4/U6.U5 tri-snRNP particles. Journal of Biological Chemistry, 317(5), 631-649. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WK7-45MGMXB-C-1&_cdi=6899&_user=38661&_pii=S0022283602954513&_origin=search&_coverDate=04%2F12%2F2002&_sk=996829994&view=c&wchp=dGLzVtb-zSkzV&md5=9f6568759a3ba0d9c6001bca1ccb2592&ie=/sdarticle.pdf.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F4DD-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E3F0-3
Genre: Journal Article

Files

show Files
hide Files
:
32817.pdf (Publisher version), 0B
Name:
32817.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Mougin, A., Author
Gottschalk, A., Author
Fabrizio, P.1, Author              
Luehrmann, R.1, Author              
Branlant, C., Author
Affiliations:
1Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              

Content

show
hide
Free keywords: -
 Abstract: The U4/U6.U5 tri-snRNP is a key component of spliceosomes. By using chemical reagents and RNases, we performed the first extensive experimental analysis of the structure and accessibility of U4 and U6 snRNAs in tri-snRNPs. These were purified from HeLa cell nuclear extract and Saccharomyces cerevisiae cellular extract. U5 accessibility was also investigated. For both species, data demonstrate the formation of the U4/U6 Y-shaped structure. In the human tri-snRNP and U4/U6 snRNP, U6 forms the long range interaction, that was previously proposed to be responsible for dissociation of the deproteinized U4/U6 duplex. In both yeast and human tri-snRNPs, U5 is more protected than U4 and U6, suggesting that the U5 snRNP-specific protein complex and other components of the tri-snRNP wrapped the 5' stem-loop of U5. Loop I of U5 is partially accessible, and chemical modifications of loop I were identical in yeast and human tri-snRNPs. This reflects a strong conservation of the interactions of proteins with the functional loop I. Only some parts of the U4/U6 Y-shaped motif (the 5' stem-loop of U4 and helix II) are protected. Due to difference of protein composition of yeast and human tri-snRNP, the U6 segment linking the 5' stem-loop to the Y-shaped structure and the U4 central single-stranded segment are more accessible in the yeast than in the human tri-snRNP, especially, the phylogenetically conserved ACAGAG sequence of U6. Data are discussed taking into account knowledge on RNA and protein components of yeast and human snRNPs and their involvement in splicesome assembly.

Details

show
hide
Language(s): eng - English
 Dates: 2002
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biological Chemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 317 (5) Sequence Number: - Start / End Page: 631 - 649 Identifier: -