A cis-acting peptide signal in human immunodeficiency virus type I Rev which inhibits nuclear entry of small proteins

Satoshi Kubota, Roger J. Pomerantz

Research output: Contribution to journalArticle

18 Citations (Scopus)


A peptide signal, which may control nucleo-cytoplasmic protein trafficking, was newly identified in human immunodeficiency virus type I (HIV-1) Rev, a lentiviral post-transcriptional transactivator. The sequence, in the amino-terminal portion of HIV-1 Rev, maintains a Rev mutant with a dysfunctional nuclear/nucleolar targeting signal outside of the nucleus, although this Rev molecule itself is small enough to pass through the nuclear pores. Transition of this sequence to the N-terminus of human T-lymphocytic leukemia/lymphoma virus type I (HTLV-I) p21(x), which is usually located evenly distributed throughout the cell, resulted in capture of p21(x) in the cytoplasm. Mutational analysis clarified that a 14 residue peptide sequence was sufficient to display this inhibitory effect against nuclear entry. Furthermore, this HIV-I Rev sequence was capable of inhibiting nuclear entry of a fragment of a human ribosomal protein, when it was fused to the carboxy terminus. The identified nuclear entry inhibitory signal (NIS) contains a conserved hydrophilicity motif, which forms an amphipathic helix. Significantly, this motif and its helical structure were shown to be important for NIS function and the HIV-1 Rev function itself. Possible roles for NIS as a molecular anchor are proposed herein.

Original languageEnglish
Pages (from-to)1851-1861
Number of pages11
Issue number14
Publication statusPublished - Apr 9 1998
Externally publishedYes



  • Entry
  • HIV-1
  • Nucleus
  • Rev
  • Transport

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

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