Skip Navigation

This Article
Right arrow Print PDF (6722K)
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 (22)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Woppmann, A.
Right arrow Articles by Lührmann, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Woppmann, A.
Right arrow Articles by Lührmann, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1988, Vol. 16, No. 23 10985-11004
© 1988

MOLECULAR BIOLOGY

Direct cross-linking of snRNP proteins F and 70K to snRNAs by ultra-violet radiation in situ

Andreas Woppmann, Jutta Rinke and Reinhard Lührmann

Max-Planck-Institut für Molekulare Genetik, Otto Warburg Laboratories D-1000 Berlin 33, FRG

Received September 27, 1988. Revised November 8, 1988. Accepted November 8, 1988.

Protein-RNA interactions in small nuclear ribonucleoproteins (UsnRNPs) from HE1A cells were investigated by irradiation of purified nucleoplasmic snRNPs U1 to U6 with UV light at 254 nm. The cross-linked proteins were analyzed on one- and two-dimensional gel electrophoresis systems, and the existence of a stable cross-linkage was demonstrated by isolating protein-oligonucleotide complexes from snRNPs containing 32 snRNAs after exhaustive digestion with a mixture of RNases of different specificities. The primary target of the UV-light induced cross-linking reaction between protein and RNA was protein F. It was also found to be cross-linked to U1 snRNA in purified U1 snRNPs. Protein F is known to be one of the common snRNP proteins, which together with D, E and G protect a 15-25 nucleotide long stretch of snRNAs U1, U2, U4 and U5, the so-called domain A or Sm binding site against nuclease digestion (Liautard et al., 1982). It is therefore likely that the core-protein may bind directly and specifically to the common SnRNA domain A, or else to a sub-region of this. The second protein which was demonstrated to be cross-linked to snRNA was the U1 specific protein 70K. Since it has been shown that binding of protein 70K to U1 RNP requires the presence of the 5' stem and loop of U1 RNA (Hamm et al., 1987) it is likely that the 70K protein directly interacts with a sub-region of the first stem loop structure.


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
 Genes Dev.Home page
K P Watkins and N Agabian
In vivo UV cross-linking of U snRNAs that participate in trypanosome trans-splicing.
Genes & Dev., October 1, 1991; 5(10): 1859 - 1869.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
H. Urlaub, K. Hartmuth, S. Kostka, G. Grelle, and R. Luhrmann
A General Approach for Identification of RNA-Protein Cross-linking Sites within Native Human Spliceosomal Small Nuclear Ribonucleoproteins (snRNPs). ANALYSIS OF RNA-PROTEIN CONTACTS IN NATIVE U1 AND U4/U6.U5 snRNPs
J. Biol. Chem., December 22, 2000; 275(52): 41458 - 41468.
[Abstract] [Full Text] [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.