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Rapid, optimized interactomic screening

Hakhverdyan, Z., Domanski, M., Hough, L. E., Oroskar, A. A., Oroskar, A. R., Keegan, S., Dilworth, D. J., Molloy, K. R., Sherman, V., Aitchison, J. D., Fenyoe, D., Chait, B. T., Jensen, T. H., Rout, M. P. & LaCava, J., 4-May-2015, In : Nature Methods. 12, 6, p. 553-560 10 p.

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  • Rapid, optimized interactomic screening

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DOI

  • Zhanna Hakhverdyan
  • Michal Domanski
  • Loren E. Hough
  • Asha A. Oroskar
  • Anil R. Oroskar
  • Sarah Keegan
  • David J. Dilworth
  • Kelly R. Molloy
  • Vadim Sherman
  • John D. Aitchison
  • David Fenyoe
  • Brian T. Chait
  • Torben Heick Jensen
  • Michael P. Rout
  • John LaCava

We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.

Original languageEnglish
Pages (from-to)553-560
Number of pages10
JournalNature Methods
Volume12
Issue number6
Publication statusPublished - 4-May-2015
Externally publishedYes

    Keywords

  • MASS-SPECTROMETRY, AFFINITY PURIFICATION, PROTEIN COMPLEXES, YEAST EXOSOME, MULTIPROTEIN COMPLEXES, ACTIN CYTOSKELETON, ARP2/3 COMPLEX, RNA-POLYMERASE, ORGANIZATION, NETWORK

ID: 117136944