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A more recent version of this article appeared on April 1, 2005 Originally published as MBC in Press, 10.1091/mbc.E04-07-0583 on January 19, 2005
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Submitted on July 13, 2004
Accepted on January 11, 2005
*Laboratory of Nucleopore Biology, Institute of Molecular and Cell Biology, Singapore 138673, Republic of Singapore; Laboratory of Molecular Virology, Centre for DNA Fingerprinting and Diagnostics, Hyderabad 500076, India
Monitoring Editor: Sandra Schmid
We report that the fission yeast nucleoporin Nup124p is required for the nuclear import of both, retrotransposon Tf1-Gag as well as the retroviral HIV-1 Vpr. Failure to import Tf1-Gag into the nucleus in a nup124 null mutant resulted in complete loss of Tf1 transposition. Similarly, nuclear import of HIV-1 Vpr was impaired in nup124 null mutant strains and cells became resistant to Vpr’s cell-killing activity. On the basis of protein domain similarity, the human nucleoporin Nup153 was identified as a putative homolog of Nup124p. We demonstrate that in vitro translated Nup124p and Nup153 coimmunoprecipitate Tf1-Gag or HIV-1Vpr. Though full-length Nup153 was unable to complement the Tf1 transposition defect in a nup124 null mutant, we provide evidence that both nucleoporins share a unique N-terminal domain, Nup124pAA264-454 and Nup153AA448-634 that is absolutely essential for Tf1 transposition. Epigenetic overexpression of this domain in a wild-type (nup124+) background blocked Tf1 activity implying that sequences from Nup124p and the human Nup153 challenged the same pathway affecting Tf1 transposition. Our results establish a unique relationship between two analogous nucleoporins Nup124p and Nup153 wherein the function of a common domain in retrotransposition is conserved.
These authors contributed equally to this work.
Corresponding author.
David Balasundaram (davidb{at}imcb.a-star.edu.sg)
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