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- Title
A cis-acting peptide signal in human immunodeficiency virus type I Rev which inhibits nuclear entry of small proteins.
- Authors
Kubota, Satoshi; Pomerantz, Roger J
- Abstract
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) p21x, which is usually located evenly distributed throughout the cell, resulted in capture of p21x 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-1 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.
- Subjects
HIV; PEPTIDES; CELL nuclei
- Publication
Oncogene, 1998, Vol 16, Issue 14, p1851
- ISSN
0950-9232
- Publication type
Article
- DOI
10.1038/sj.onc.1201738