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All four homochiral enantiomers of a nuclear localization sequence derived from c-Myc serve as functional import signals

Academic Article
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Overview

related to degree

  • Saphire, Andrew, Ph.D. in Biology, Scripps Research 1990 - 1998
  • Bark, Steven, Ph.D. in Macromolecular Structure and Chemistry, Scripps Research 1991 - 1997

authors

  • Saphire, Andrew
  • Bark, Steven
  • Gerace, Larry

publication date

  • November 1998

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The information that targets a protein to the nucleus often consists of a short cluster of basic amino acids called a nuclear localization sequence (NLS). Since a wide range of sequences rich in basic amino acid residues function as NLSs, we postulated that an NLS-like sequence composed exclusively of D-amino acids might have biological activity. We synthesized peptides corresponding to the c-Myc NLS composed of either all L or D-amino acids, both in the forward and reverse order. We tested these peptides for nuclear import activity in a digitonin-permeabilized cell assay. All four peptide-bovine serum albumin conjugates localized to the nucleus with similar efficiency, and each conjugate competed for import with an SV40 large T antigen-derived NLS conjugate. Cross-linking experiments with free NLS peptides in HeLa cytosol indicated that each peptide bound to a protein that migrated at the molecular weight of importin alpha. Recombinant importin alpha, importin beta, Ran, and NTF2 alone were sufficient to support the import of both L-form and D-form conjugates in permeabilized cells. This indicates that both D- and L-form NLS peptides use the same import machinery. Although the free D-forms of the NLS were proteolytically resistant in cytosol, the L-forms were rapidly degraded. To our knowledge, this is the first example of an intracellular pathway in which the receptor is insensitive to the chirality of the ligand.

subject areas

  • Antigens, Polyomavirus Transforming
  • Biological Transport
  • HeLa Cells
  • Humans
  • Nuclear Localization Signals
  • Proto-Oncogene Proteins c-myc
  • Simian virus 40
  • Stereoisomerism
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.273.45.29764

PubMed ID

  • 9792690
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Additional Document Info

start page

  • 29764

end page

  • 29769

volume

  • 273

issue

  • 45

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