| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 280, Issue 16, 16066-16075, April 22, 2005
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
¶
From the
Paul Scherrer Institut, Biomolecular Research, CH5232 Villigen and the M. E. Müller Institute for Microscopy, Biozentrum, the University of Basel, Klingelbergstrasse 70, CH4056 Basel, Switzerland
Sm and Sm-like (LSm) proteins form complexes engaging in various RNA-processing events. Composition and architecture of the complexes determine their intracellular distribution, RNA targets, and function. We have reconstituted the human LSm1–7 and LSm2–8 complexes from their constituent components in vitro. Based on the assembly pathway of the canonical Sm core domain, we used heterodimeric and heterotrimeric sub-complexes to assemble LSm1–7 and LSm2–8. Isolated sub-complexes form ring-like higher order structures. LSm1–7 is assembled and stable in the absence of RNA. LSm1–7 forms ring-like structures very similar to LSm2–8 at the EM level. Our in vitro reconstitution results illustrate likely features of the LSm complex assembly pathway. We prove the complexes to be functional both in an RNA bandshift and an in vivo cellular transport assay.
Received for publication, December 22, 2004 , and in revised form, February 7, 2005.
* This work was supported by the Swiss National Fund (SNF), Grant Nr. 3100-062018 and the Swiss National Center of Competence in Research (NCCR) in Structural Biology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http//www.jbc.org) contains Supplemental Fig. S1.
¶ To whom correspondence should be addressed: Life Sciences, OFLC 110, Paul Scherrer Institut, CH5232 Villigen PSI, Switzerland. Tel.: 41-56-310-4723; Fax: 41-56-310-5288; E-mail: christian.kambach{at}psi.ch.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Licht, J. Medenbach, R. Luhrmann, C. Kambach, and A. Bindereif 3'-cyclic phosphorylation of U6 snRNA leads to recruitment of recycling factor p110 through LSm proteins RNA, August 1, 2008; 14(8): 1532 - 1538. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. M. Watson, S. W. Miller, M. Fraig, D. J. Cole, D. K. Watson, and A. M. Boylan CaSm (LSm-1) Overexpression in Lung Cancer and Mesothelioma Is Required for Transformed Phenotypes Am. J. Respir. Cell Mol. Biol., June 1, 2008; 38(6): 671 - 678. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. P. Spiller, M. A. M. Reijns, and J. D. Beggs Requirements for nuclear localization of the Lsm2-8p complex and competition between nuclear and cytoplasmic Lsm complexes J. Cell Sci., December 15, 2007; 120(24): 4310 - 4320. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Chowdhury, J. Mukhopadhyay, and S. Tharun The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs RNA, July 1, 2007; 13(7): 998 - 1016. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Fleurdepine, J.-M. Deragon, M. Devic, J. Guilleminot, and C. Bousquet-Antonelli A bona fide La protein is required for embryogenesis in Arabidopsis thaliana Nucleic Acids Res., May 11, 2007; 35(10): 3306 - 3321. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
