This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Preußer, C.
Right arrow Articles by Bindereif, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Preußer, C.
Right arrow Articles by Bindereif, A.

 Previous Article  |  Next Article 

Eukaryotic Cell, August 2009, p. 1228-1234, Vol. 8, No. 8
1535-9778/09/$08.00+0     doi:10.1128/EC.00090-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Special Sm Core Complex Functions in Assembly of the U2 Small Nuclear Ribonucleoprotein of Trypanosoma brucei{triangledown} ,{dagger}

Christian Preußer, Zsofia Palfi, and Albrecht Bindereif*

Institute of Biochemistry, Justus Liebig University of Giessen, D-35392 Giessen, Germany

Received 19 March 2009/ Accepted 9 June 2009

The processing of polycistronic pre-mRNAs in trypanosomes requires the spliceosomal small ribonucleoprotein complexes (snRNPs) U1, U2, U4/U6, U5, and SL, each of which contains a core of seven Sm proteins. Recently we reported the first evidence for a core variation in spliceosomal snRNPs; specifically, in the trypanosome U2 snRNP, two of the canonical Sm proteins, SmB and SmD3, are replaced by two U2-specific Sm proteins, Sm15K and Sm16.5K. Here we identify the U2-specific, nuclear-localized U2B'' protein from Trypanosoma brucei. U2B'' interacts with a second U2 snRNP protein, U2-40K (U2A'), which in turn contacts the U2-specific Sm16.5K/15K subcomplex. Together they form a high-affinity, U2-specific binding complex. This trypanosome-specific assembly differs from the mammalian system and provides a functional role for the Sm core variation found in the trypanosomal U2 snRNP.

* Corresponding author. Mailing address: Institute of Biochemistry, Justus Liebig University of Giessen, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany. Phone: 49 - 641 - 9935 420. Fax: 49 - 641 - 9935 419. E-mail: albrecht.bindereif{at}chemie.bio.uni-giessen.de

{triangledown} Published ahead of print on 19 June 2009.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, August 2009, p. 1228-1234, Vol. 8, No. 8
1535-9778/09/$08.00+0     doi:10.1128/EC.00090-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Palfi, Z., Jae, N., Preusser, C., Kaminska, K. H., Bujnicki, J. M., Lee, J. H., Gunzl, A., Kambach, C., Urlaub, H., Bindereif, A. (2009). SMN-assisted assembly of snRNP-specific Sm cores in trypanosomes. Genes Dev. 23: 1650-1664 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»