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Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold

By Maria R. Conte, Tim Grüne, Jamie Ghuman, Geoff Kelly, Anastasia Ladas, Stephen Matthews and Stephen Curry

Abstract

Polypyrimidine tract binding protein (PTB), an RNA binding protein containing four RNA recognition motifs (RRMs), is involved in both pre-mRNA splicing and translation initiation directed by picornaviral internal ribosome entry sites. Sequence comparisons previously indicated that PTB is a non-canonical RRM protein. The solution structure of a PTB fragment containing RRMs 3 and 4 shows that the protein consists of two domains connected by a long, flexible linker. The two domains tumble independently in solution, having no fixed relative orientation. In addition to the βαββαβ topology, which is characteristic of RRM domains, the C-terminal extension of PTB RRM-3 incorporates an unanticipated fifth β-strand, which extends the RNA binding surface. The long, disordered polypeptide connecting β4 and β5 in RRM-3 is poised above the RNA binding surface and is likely to contribute to RNA recognition. Mutational analyses show that both RRM-3 and RRM-4 contribute to RNA binding specificity and that, despite its unusual sequence, PTB binds RNA in a manner akin to that of other RRM proteins

Topics: Articles
Publisher: Oxford University Press
Year: 2000
DOI identifier: 10.1093/emboj
OAI identifier: oai:pubmedcentral.nih.gov:203357
Provided by: PubMed Central
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