Skip Navigation

This Article
Right arrow Print PDF (3235K)
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 arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Nelissen, R. L.H.
Right arrow Articles by Venrooij, W. J.v.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nelissen, R. L.H.
Right arrow Articles by Venrooij, W. J.v.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1991, Vol. 19, No. 3 449-454
© 1991


MOLECULAR BIOLOGY

Zinc finger-like structure in U1-specific protein C is essential for specific binding to U1 snRNP

Rob L.H. Nelissen*, Volker Heinrichs1, Winand J. Habets, Frank Simons, Reinhard L{euro}hrmann1 and Walther J.van Venrooij

1Institut f{euro}r Molekularbiologie und Tumorforschung Emil Mannkopff Strasse 2, D 3550 Marburg, FRG Department of Biochemistry, University of Nijmegen PO Box 9101, NL 6500 HB Nijmegen, The Netherlands

*To whom correspondence should be addressed

Received November 26, 1990. Accepted January 7, 1991.

The U1 small nuclear ribonucleoprotein (snRNP) contains three specific proteins denoted 70K, A and C, in addition to the common proteins. Specific functions of these proteins are not known although recently protein C was shown to be Involved in the binding of U1 snRNP to the 5' splice site of a pre-mRNA. Unlike proteins A and 70K, U1-C lacks an RNA binding domain (RNP-80 motif) and does not appear to bind directly to U1 snRNA. However, at the amino terminal end protein C contains a zinc finger-like structure of the CC-HH type found in transcription factor TF IDA. Several lines of evidence indicate that the zinc finger-like structure is essential for the binding of protein C to U1 snRNP particles: i) deletion analysis of protein C showed that the N-terminal 45 amino acids are sufficient for binding to U1 snRNPs, II) modification of the cystelne residues In the N-terminal domain with N-ethylmaleimide and lii) single point mutations of the cysteines and hlstidines contributing to the putative zinc finger abolished binding of protein C to U1 snRNPs. Interestingly, unlike the proteins U1-A and U1-70K the U1-C protein is unable to bind to naked U1 snRNA. On the other hand it is shown that protein C does not bind to the known protein constituents of the U1 particle without the U1 snRNA being present. These data indicate that the binding of protein C to U1 snRNP is dependent on the presence of both the U1 snRNA and one or more of the U1 snRNP proteins.


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
Nucleic Acids ResHome page
Z. Palfi, B. Schimanski, A. Gunzl, S. Lucke, and A. Bindereif
U1 small nuclear RNP from Trypanosoma brucei: a minimal U1 snRNA with unusual protein components
Nucleic Acids Res., April 29, 2005; 33(8): 2493 - 2503.
[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
Proc. Natl. Acad. Sci. USAHome page
M. T. Bedford, R. Reed, and P. Leder
WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: The proline glycine and methionine-rich motif
PNAS, September 1, 1998; 95(18): 10602 - 10607.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
P Legrain and C Chapon
Interaction between PRP11 and SPP91 yeast splicing factors and characterization of a PRP9-PRP11-SPP91 complex
Science, October 1, 1993; 262(5130): 108 - 110.
[Abstract] [PDF]


Home page
Genes Dev.Home page
P Legrain, C Chapon, and F Galisson
Interactions between PRP9 and SPP91 splicing factors identify a protein complex required in prespliceosome assembly.
Genes & Dev., July 1, 1993; 7(7b): 1390 - 1399.
[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.