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Classical NLS proteins from Saccharomyces cerevisiae.

Silvia Hahn1, Patrick Maurer, Stefanie Caesar

  • 1Medizinische Biochemie und Molekularbiologie, Universität des Saarlandes, Geb. 61.4, 66421 Homburg, Germany.

Journal of Molecular Biology
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Summary
This summary is machine-generated.

Five yeast proteins are confirmed as nuclear import cargos via the classical nuclear localization signal (cNLS) pathway. This pathway involves importin alpha (Impalpha) and importin beta (Impbeta), with Nup2 crucial for import termination.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Nuclear proteins are imported via receptor-mediated pathways, including those using classical nuclear localization signals (cNLS).
  • The importin alpha (Impalpha)/importin beta (Impbeta) pathway is critical for translocating cNLS-containing proteins through the nuclear pore complex.
  • Defining authentic yeast cNLS cargos requires demonstrating in vivo import defects and direct binding to Impalpha, stimulated by Impbeta.

Purpose of the Study:

  • To identify and validate endogenous Saccharomyces cerevisiae proteins that utilize the classical nuclear localization signal (cNLS) import pathway.
  • To characterize the nature of cNLS signals in identified proteins and determine binding affinities within the import complex.
  • To elucidate the role of Impbeta and Nup2 in the nuclear import and termination processes.

Main Methods:

  • In vivo import defect assays in Impalpha and Impbeta mutants.
  • Surface plasmon resonance spectrometry to determine binding constants of cNLS/Impalpha/Impbeta complexes.
  • Analysis of Nup2's role in the import of validated cNLS cargos.

Main Results:

  • Prp20, Cdc6, Swi5, Cdc45, and Clb2 were confirmed as authentic yeast cNLS cargos.
  • Prp20 possesses a bipartite cNLS, while Cdc6 has a monopartite cNLS, with varying significance of basic residues for Impalpha interaction.
  • Dissociation constants (Kd) for cNLS/Impalpha/Impbeta complexes ranged from 1 nM (Cdc6) to 112 nM (Swi5), indicating import kinetics are influenced by cNLS/Impalpha binding strength. Impbeta enhanced Impalpha affinity ~100-fold via faster association. Nup2 is required for efficient import of all identified cNLS cargos.

Conclusions:

  • The study validates five new yeast proteins as cNLS cargos, expanding the known repertoire of nuclear import substrates.
  • Binding affinities and the stimulatory role of Impbeta highlight the intricate regulation of nuclear import efficiency.
  • Nup2 plays a general role in terminating nuclear import by facilitating the dissociation of cNLS/Impalpha complexes.