WeightNameValue
1000 Titel
  • Multivalent Binding of Formin-binding Protein 21 (FBP21)-Tandem-WW Domains Fosters Protein Recognition in the Pre-spliceosome
1000 Autor/in
  1. Klippel, Stefan |
  2. Wieczorek, Marek |
  3. Schümann, Michael |
  4. Krause, Eberhard |
  5. Marg, Berenice |
  6. Seidel, Thorsten |
  7. Meyer, Tim |
  8. Knapp, Ernst-Walter |
  9. Freund, Christian |
1000 Erscheinungsjahr 2011
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2011-09-14
1000 Erschienen in
1000 Quellenangabe
  • 286: 38478-38487
1000 FRL-Sammlung
1000 Verlagsversion
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3207436/ |
  • http://doi.org/10.1074/jbc.M111.265710 |
1000 Ergänzendes Material
  • http://www.jbc.org/content/286/44/38478/suppl/DC1 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • The high abundance of repetitive but nonidentical proline-rich sequences in spliceosomal proteins raises the question of how these known interaction motifs recruit their interacting protein domains. Whereas complex formation of these adaptors with individual motifs has been studied in great detail, little is known about the binding mode of domains arranged in tandem repeats and long proline-rich sequences including multiple motifs. Here we studied the interaction of the two adjacent WW domains of spliceosomal protein FBP21 with several ligands of different lengths and composition to elucidate the hallmarks of multivalent binding for this class of recognition domains. First, we show that many of the proteins that define the cellular proteome interacting with FBP21-WW1-WW2 contain multiple proline-rich motifs. Among these is the newly identified binding partner SF3B4. Fluorescence resonance energy transfer (FRET) analysis reveals the tandem-WW domains of FBP21 to interact with splicing factor 3B4 (SF3B4) in nuclear speckles where splicing takes place. Isothermal titration calorimetry and NMR shows that the tandem arrangement of WW domains and the multivalency of the proline-rich ligands both contribute to affinity enhancement. However, ligand exchange remains fast compared with the NMR time scale. Surprisingly, a N-terminal spin label attached to a bivalent ligand induces NMR line broadening of signals corresponding to both WW domains of the FBP21-WW1-WW2 protein. This suggests that distinct orientations of the ligand contribute to a delocalized and semispecific binding mode that should facilitate search processes within the spliceosome.
1000 Sacherschließung
lokal Isothermal Titration Calorimetry
lokal Spliceosome
lokal NMR
lokal Multivalent
lokal Mass Spectrometry (MS)
lokal Protein Domains
lokal Spin-label
lokal WW Domain
1000 Fachgruppe
  1. Biologie |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/S2xpcHBlbCwgU3RlZmFu|https://frl.publisso.de/adhoc/creator/V2llY3pvcmVrLCBNYXJlaw==|https://frl.publisso.de/adhoc/creator/U2Now7xtYW5uLCBNaWNoYWVs|https://frl.publisso.de/adhoc/creator/S3JhdXNlLCBFYmVyaGFyZA==|https://frl.publisso.de/adhoc/creator/TWFyZywgQmVyZW5pY2U=|https://frl.publisso.de/adhoc/creator/U2VpZGVsLCBUaG9yc3Rlbg==|https://frl.publisso.de/adhoc/creator/TWV5ZXIsIFRpbQ==|https://frl.publisso.de/adhoc/creator/S25hcHAsIEVybnN0LVdhbHRlcg==|https://frl.publisso.de/adhoc/creator/RnJldW5kLCBDaHJpc3RpYW4=
1000 Förderer
  1. Deutsche Forschungsgemeinschaft |
1000 Fördernummer
  1. FG806; SFB765
1000 Förderprogramm
  1. -
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer Deutsche Forschungsgemeinschaft |
    1000 Förderprogramm -
    1000 Fördernummer FG806; SFB765
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6403015.rdf
1000 Erstellt am 2017-06-13T11:07:36.964+0200
1000 Erstellt von 25
1000 beschreibt frl:6403015
1000 Bearbeitet von 218
1000 Zuletzt bearbeitet Wed May 30 12:06:12 CEST 2018
1000 Objekt bearb. Wed May 30 12:06:12 CEST 2018
1000 Vgl. frl:6403015
1000 Oai Id
  1. oai:frl.publisso.de:frl:6403015 |
1000 Sichtbarkeit Metadaten public
1000 Sichtbarkeit Daten public
1000 Gegenstand von

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