Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (573K) Freely available
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 ISI Web of Science
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 (14)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Yuan, X.
Right arrow Articles by Matthews, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yuan, X.
Right arrow Articles by Matthews, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2002, Vol. 30, No. 2 456-462
© 2002 Oxford University Press

Chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein

Xuemei Yuan1, Natalia Davydova2, Maria R. Conte, Stephen Curry2,* and Stephen Matthews1

Department of Biological Sciences and Centre for Structural Biology, Imperial College of Science, Technology and Medicine, 1Wolfson Laboratory, Exhibition Road, London SW7 2AY, UK and 2Blackett Laboratory, Prince Consort Road, London SW7 2BW, UK

The polypyrimidine tract binding protein (PTB), a homodimer that contains four RRM-type RNA binding domains per monomer, plays important roles in both the regulation of alternative splicing and the stimulation of translation initiation as directed by the internal ribosome entry sites of certain picornaviruses. We have used chemical shift mapping experiments to probe the interactions between PTB-34, a recombinant fragment that contains the third and fourth RRM domains of the protein, and a number of short pyrimidine-rich RNA oligonucleotides. The results confirm that the RNAs interact primarily with the ß-sheet surface of PTB-34, but also reveal roles for the two long flexible linkers within the protein fragment, a result that is supported by mutagenesis experiments. The mapping indicates distinct binding preferences for RRM3 and RRM4 with the former making a particularly specific interaction with the sequence UCUUC.

* To whom correspondence should be addressed. Tel: +44 207 594 7632; Fax: +44 207 589 0191; Email: s.curry@ic.ac.uk Correspondence may also be addressed to Stephen Matthews. Tel: +44 207 594 5315; Fax: +44 207 594 5225; Email: s.j.matthews{at}ic.ac.uk Present address:Maria R. Conte, Biophysics Laboratories, St Michael’s Building, University of Portsmouth, White Swan Road, Portsmouth PO1 2DT, UK


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
L. H. Matzat, S. Berberoglu, and L. Levesque
Formation of a Tap/NXF1 Homotypic Complex Is Mediated through the Amino-Terminal Domain of Tap and Enhances Interaction with Nucleoporins
Mol. Biol. Cell, January 1, 2008; 19(1): 327 - 338.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
C. CLERTE and K. B. HALL
Characterization of multimeric complexes formed by the human PTB1 protein on RNA
RNA, March 1, 2006; 12(3): 457 - 475.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
Y. SONG, E. TZIMA, K. OCHS, G. BASSILI, H. TRUSHEIM, M. LINDER, K. T. PREISSNER, and M. NIEPMANN
Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation
RNA, December 1, 2005; 11(12): 1809 - 1824.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
B. AMIR-AHMADY, P. L. BOUTZ, V. MARKOVTSOV, M. L. PHILLIPS, and D. L. BLACK
Exon repression by polypyrimidine tract binding protein
RNA, May 1, 2005; 11(5): 699 - 716.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
N. A. Faustino and T. A. Cooper
Identification of Putative New Splicing Targets for ETR-3 Using Sequences Identified by Systematic Evolution of Ligands by Exponential Enrichment
Mol. Cell. Biol., February 1, 2005; 25(3): 879 - 887.
[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.