Skip Navigation

This Article
Right arrow Print PDF (3839K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email 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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (26)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kramer, A.
Right arrow Articles by Bilbe, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kramer, A.
Right arrow Articles by Bilbe, G.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1994, Vol. 22, No. 24 5223-5228
© 1994


Articles

Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo

Angela Kramer*,, Pierre Legrain1, Frank Mulhauser, Karsten Groöining, Reto Brosi and Graeme Bilbe2

Deépartement de Biologie Cellulaire, Universiteé de Geneéve, 30 quai Ernest-Ansermet, CH-1211 Geneéve 4, Switzerland 1Deépartement de Biologie Moleéculaire, Institut Pasteur 25 rue du Dr Roux, F-75724 Paris Cedex 15, France 2Pharma Research, Department of Molecular and Cell Biology Ciba-Geigy Ltd, CH-4002 Basel, Switzerland

*To whom correspondence should be addressed

Received September 23, 1994. Accepted October 28, 1994.

A cDNA encoding the 60 kDa subunit of mammalian splicing factor SF3a has been isolated. The deduced protein sequence reveals a 30% Identity to the PRP9 splicing protein of the yeast S.cerevisiae. The highest homology is present In a zinc finger-like region In the C-terminal domain of both proteins. The PRP9 zinc finger-like motif has been replaced by the equivalent region of mammalian SF3a60. The chlmerlc protein rescues the temperature-sensitive phenotype of the prp9-1 mutant strain demonstrating that not only the structure but also the function of this domain has been conserved during evolution.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Mol. Biol. CellHome page
G. Tanackovic and A. Kramer
Human Splicing Factor SF3a, but Not SF1, Is Essential for Pre-mRNA Splicing In Vivo
Mol. Biol. Cell, March 1, 2005; 16(3): 1366 - 1377.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
D. Nesic, G. Tanackovic, and A. Kramer
A role for Cajal bodies in the final steps of U2 snRNP biogenesis
J. Cell Sci., September 1, 2004; 117(19): 4423 - 4433.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
D. Nesic and A. Kramer
Domains in Human Splicing Factors SF3a60 and SF3a66 Required for Binding to SF3a120, Assembly of the 17S U2 snRNP, and Prespliceosome Formation
Mol. Cell. Biol., October 1, 2001; 21(19): 6406 - 6417.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
D. Yan, R. Perriman, H. Igel, K. J. Howe, M. Neville, and M. Ares Jr.
CUS2, a Yeast Homolog of Human Tat-SF1, Rescues Function of Misfolded U2 through an Unusual RNA Recognition Motif
Mol. Cell. Biol., September 1, 1998; 18(9): 5000 - 5009.
[Abstract] [Full Text]


Home page
Mol. Cell. Biol.Home page
V. Meyer, B. Oliver, and D. Pauli
Multiple Developmental Requirements of Noisette, the Drosophila Homolog of the U2 snRNP-Associated Polypeptide SF3a60
Mol. Cell. Biol., April 1, 1998; 18(4): 1835 - 1843.
[Abstract] [Full Text]


Home page
Mol. Cell. Biol.Home page
W.-J. Zhang and J. Y. Wu
Sip1, a Novel RS Domain-Containing Protein Essential for Pre-mRNA Splicing
Mol. Cell. Biol., February 1, 1998; 18(2): 676 - 684.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
D. K. Wiest, C. L. O'Day, and J. Abelson
In Vitro Studies of the Prp9·Prp11·Prp21 Complex Indicate a Pathway for U2 Small Nuclear Ribonucleoprotein Activation
J. Biol. Chem., December 27, 1996; 271(52): 33268 - 33276.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
S E Wells, M Neville, M Haynes, J Wang, H Igel, and M Ares
CUS1, a suppressor of cold-sensitive U2 snRNA mutations, is a novel yeast splicing factor homologous to human SAP 145.
Genes & Dev., January 15, 1996; 10(2): 220 - 232.
[Abstract] [PDF]


Home page
Genes Dev.Home page
O Gozani, R Feld, and R Reed
Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A.
Genes & Dev., January 15, 1996; 10(2): 233 - 243.
[Abstract] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.