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Molecular and Cellular Biology, December 2000, p. 8996-9008, Vol. 20, No. 23
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

TAP (NXF1) Belongs to a Multigene Family of Putative RNA Export Factors with a Conserved Modular Architecture

Andrea Herold,1 Mikita Suyama,1 João P. Rodrigues,2 Isabelle C. Braun,1 Ulrike Kutay,3 Maria Carmo-Fonseca,2 Peer Bork,1 and Elisa Izaurralde1,*

European Molecular Biology Laboratory, D-69117 Heidelberg, Germany1; Institute of Histology and Embryology, Faculty of Medicine, University of Lisbon, 1699 Lisbon Codex, Portugal2; and Institute of Biochemistry, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland3

Received 12 July 2000/Returned for modification 15 August 2000/Accepted 6 September 2000

Vertebrate TAP (also called NXF1) and its yeast orthologue, Mex67p, have been implicated in the export of mRNAs from the nucleus. The TAP protein includes a noncanonical RNP-type RNA binding domain, four leucine-rich repeats, an NTF2-like domain that allows heterodimerization with p15 (also called NXT1), and a ubiquitin-associated domain that mediates the interaction with nucleoporins. Here we show that TAP belongs to an evolutionarily conserved family of proteins that has more than one member in higher eukaryotes. Not only the overall domain organization but also residues important for p15 and nucleoporin interaction are conserved in most family members. We characterize two of four human TAP homologues and show that one of them, NXF2, binds RNA, localizes to the nuclear envelope, and exhibits RNA export activity. NXF3, which does not bind RNA or localize to the nuclear rim, has no RNA export activity. Database searches revealed that although only one p15 (nxt) gene is present in the Drosophila melanogaster and Caenorhabditis elegans genomes, there is at least one additional p15 homologue (p15-2 [also called NXT2]) encoded by the human genome. Both human p15 homologues bind TAP, NXF2, and NXF3. Together, our results indicate that the TAP-p15 mRNA export pathway has diversified in higher eukaryotes compared to yeast, perhaps reflecting a greater substrate complexity.

* Corresponding author. Mailing address: EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. Phone: 0049 6221 387 389. Fax: 0049 6221 387 518. E-mail: izaurralde{at}embl-heidelberg.de.

Molecular and Cellular Biology, December 2000, p. 8996-9008, Vol. 20, No. 23
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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