Evolutionary specialization of the nuclear targeting apparatus

  1. Harmit S. Malik,
  2. Thomas H. Eickbush, and
  3. David S. Goldfarb*
  1. Department of Biology, University of Rochester, Rochester, NY 14627
  1. Communicated by Masayasu Nomura, University of California, Irvine, CA (received for review August 1, 1997)

Abstract

The α- and β-karyopherins (Kaps), also called importins, mediate the nuclear transport of proteins. All α-Kaps contain a central domain composed of eight approximately 40 amino acid, tandemly arranged, armadillo-like (Arm) repeats. The number and order of these repeats have not changed since the common origin of fungi, plants, and mammals. Phylogenetic analysis suggests that the various α-Kaps fall into two groups, α1 and α2. Whereas animals encode both types, the yeast genome encodes only an α1-Kap. The β-Kaps are characterized by 14–15 tandemly arranged HEAT motifs. We show that the Arm repeats of α-Kaps and the HEAT motifs of β-Kaps are similar, suggesting that the α-Kaps and β-Kaps (and for that matter, all Arm and HEAT repeat-containing proteins) are members of the same protein superfamily. Phylogenetic analysis indicates that there are at least three major groups of β-Kaps, consistent with their proposed cargo specificities. We present a model in which an α-independent β-Kap progenitor gave rise to the α-dependent β-Kaps and the α-Kaps.

Footnotes

  • * To whom reprint requests should be addressed. e-mail: Goldfarb{at}Nucleus.Biology.Rochester.edu.

  • ABBREVIATIONS:
    Kap,
    karyopherin;
    Arm,
    armadillo;
    NLS,
    nuclear localization signal
« Previous | Next Article »Table of Contents