Induced folding of the U2AF35 RRM upon binding to U2AF65

Kellenberger, Esther; Stier, Gunter; Sattler, Michael

doi:10.1016/S0014-5793(02)03294-5

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Induced folding of the U2AF35 RRM upon binding to U2AF65

MPS-Authors

/persons/resource/persons117899

Stier, Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1016/S0014-5793%2802%2903294-5
(Any fulltext)

https://doi.org/10.1016/S0014-5793(02)03294-5
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Kellenberger, E., Stier, G., & Sattler, M. (2002). Induced folding of the U2AF35 RRM upon binding to U2AF65. FEBS Letters, 528(1), 171-176. doi:10.1016/S0014-5793(02)03294-5.

Cite as: https://hdl.handle.net/21.11116/0000-0001-EF72-2

Abstract

The human essential splicing factor U2AF (U2 auxiliary factor) consists of 35 and 65 kDa subunits which form a highly stable heterodimer in solution. Copurification of the recombinant U2AF35 RNA recognition motif (U2AF35 RRM) and full-length U2AF65 yields a soluble and functionally active minimal U2AF heterodimer. Recombinant U2AF35 RRM protein free and in complex with three different regions of U2AF65 was characterized by nuclear magnetic resonance spectroscopy. We found that the recombinant U2AF35 RRM is unstructured in solution but its tertiary structure is induced upon binding to U2AF65. This interaction is mediated by the N-terminal proline-rich region of U2AF65 and does not involve the U2AF65 RRMs.