Induced folding of the U2AF35 RRM upon binding to U2AF65

Esther Kellenberger; Gunter Stier; Michael Sattler

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

Induced folding of the U2AF35 RRM upon binding to U2AF65

Esther Kellenberger, Gunter Stier, Michael Sattler

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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.

Original language	English
Pages (from-to)	171-176
Number of pages	6
Journal	FEBS Letters
Volume	528
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03294-5
State	Published - 25 Sep 2002
Externally published	Yes

Keywords

Folding
Nuclear magnetic resonance
RNA recognition motif
Splicing
U2 auxiliary factor

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10.1016/S0014-5793(02)03294-5

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@article{3911314ec17343fe8dddcaeeab708908,

title = "Induced folding of the U2AF35 RRM upon binding to U2AF65",

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.",

keywords = "Folding, Nuclear magnetic resonance, RNA recognition motif, Splicing, U2 auxiliary factor",

author = "Esther Kellenberger and Gunter Stier and Michael Sattler",

note = "Funding Information: We thank Juan Valc{\'a}rcel, Gilles Trav{\'e}, Katia Zanier, Alexander Gasch, Philipp Selenko and members of the EMBL NMR group for advice, discussions and critical reading of the manuscript. E.K. was supported by the Alexander von Humboldt foundation. M.S acknowledges support by the EU (D-LAB) and the DFG.",

year = "2002",

month = sep,

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doi = "10.1016/S0014-5793(02)03294-5",

language = "English",

volume = "528",

pages = "171--176",

journal = "FEBS Letters",

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number = "1-3",

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T1 - Induced folding of the U2AF35 RRM upon binding to U2AF65

AU - Kellenberger, Esther

AU - Stier, Gunter

AU - Sattler, Michael

N1 - Funding Information: We thank Juan Valcárcel, Gilles Travé, Katia Zanier, Alexander Gasch, Philipp Selenko and members of the EMBL NMR group for advice, discussions and critical reading of the manuscript. E.K. was supported by the Alexander von Humboldt foundation. M.S acknowledges support by the EU (D-LAB) and the DFG.

PY - 2002/9/25

Y1 - 2002/9/25

N2 - 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.

AB - 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.

KW - Folding

KW - Nuclear magnetic resonance

KW - RNA recognition motif

KW - Splicing

KW - U2 auxiliary factor

UR - http://www.scopus.com/inward/record.url?scp=0037174170&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(02)03294-5

DO - 10.1016/S0014-5793(02)03294-5

M3 - Article

C2 - 12297299

AN - SCOPUS:0037174170

SN - 0014-5793

VL - 528

SP - 171

EP - 176

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Induced folding of the U2AF35 RRM upon binding to U2AF65

Abstract

Keywords

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