Molecular architecture of the human U4/U6.U5 tri-snRNP-Reference-Cited by-同舟云学术

Molecular architecture of the human U4/U6.U5 tri-snRNP

Published:2016-03-25 Issue:6280 Volume:351 Page:1416-1420
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Agafonov Dmitry E.¹,Kastner Berthold¹,Dybkov Olexandr¹,Hofele Romina V.²³,Liu Wen-Ti⁴⁵,Urlaub Henning²³,Lührmann Reinhard¹,Stark Holger⁴⁵

Affiliation:

1. Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.

2. Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.

3. Bioanalytics Group, Institute for Clinical Chemistry, University Medical Center Göttingen, D-37075 Göttingen, Germany.

4. Department of 3D Electron Cryomicroscopy, Georg-August Universität Göttingen, D-37077 Göttingen, Germany.

5. Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.

Abstract

A human spliceosomal subcomplex The spliceosome is an RNA and protein molecular machine that cuts out introns from messenger RNAs. Agafonov et al. used cryo-electron microscopy to determine the structure of the largest intermediate subcomplex on the assembly pathway for the human spliceosome (see the Perspective by Cate). The structure shows substantial differences from the equivalent yeast complex. It also reveals how the subcomplex must dock onto the rest of the spliceosome and hints at the structural changes the complex must go through to form the mature spliceosome. Science , this issue p. 1416 ; see also p. 1390

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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