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  Dimerization and protein binding specificity of the U2AF homology motif of the splicing factor Puf60

Corsini, L., Hothorn, M., Stier, G., Rybin, V., Scheffzek, K., Gibson, T. J., et al. (2009). Dimerization and protein binding specificity of the U2AF homology motif of the splicing factor Puf60. The Journal of Biological Chemistry, 284(1), 630-639. doi:10.1074/jbc.M805395200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-8B51-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-E39F-D
Genre: Journal Article

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JBiolChem_284_2009_630.pdf (Any fulltext), 2MB
 
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 Creators:
Corsini, Lorenzo, Author
Hothorn, Michael, Author
Stier, Gunter1, Author              
Rybin, Vladimir, Author
Scheffzek, Klaus2, Author              
Gibson, Toby J., Author
Sattler, Michael, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: PUF60 is an essential splicing factor functionally related and homologous to U2AF(65). Its C-terminal domain belongs to the family of U2AF (U2 auxiliary factor) homology motifs (UHM), a subgroup of RNA recognition motifs that bind to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. Here, we show that the Puf60 UHM is mainly monomeric in physiological buffer, whereas its dimerization is induced upon the addition of SDS. The crystal structure of PUF60-UHM at 2.2 angstroms resolution, NMR data, and mutational analysis reveal that the dimer interface is mediated by electrostatic interactions involving a flexible loop. Using glutathione S-transferase pulldown experiments, isothermal titration calorimetry, and NMR titrations, we find that Puf60-UHM binds to ULM sequences in the splicing factors SF1, U2AF65, and SF3b155. Compared with U2AF65-UHM, Puf60-UHM has distinct binding preferences to ULMs in the N terminus of SF3b155. Our data suggest that the functional cooperativity between U2AF65 and Puf60 may involve simultaneous interactions of the two proteins with SF3b155.

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Language(s): eng - English
 Dates: 2008-10-072008-07-162008-10-072008-10-292009-01-02
 Publication Status: Published in print
 Pages: 10
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 Table of Contents: -
 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 284 (1) Sequence Number: - Start / End Page: 630 - 639 Identifier: ISSN: 0021-9258
CoNE: /journals/resource/954925410826_1