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Published online 21 August 2000. doi:10.1083/jcb.150.4.695
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© The Rockefeller University Press, 0021-9525/2000/8/695/ $5.00
The Journal of Cell Biology, Volume 150, Number 4, August 21, 2000 695-706

Original Article

Binding of the Mex67p/Mtr2p Heterodimer to FXFG, GLFG, and FG Repeat Nucleoporins Is Essential for Nuclear mRNA Export

Katja Sträßera, Jochen Baßlera, and Ed Hurta
a BZH, Biochemie-Zentrum Heidelberg, D-69120 Heidelberg, Germany

Correspondence to: Ed Hurt, BZH, Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany. Tel:49 6221 54 41 73 Fax:49 6221 54 43 69 E-mail:cg5{at}ix.urz.uni-heidelberg.de.

It is not known how Mex67p and Mtr2p, which form a heterodimer essential for mRNA export, transport mRNPs through the nuclear pore. Here, we show that the Mex67p/Mtr2p complex binds to all of the repeat types (GLFG, FXFG, and FG) found in nucleoporins. For this interaction, complex formation between Mex67p and Mtr2p has to occur. MEX67 and MTR2 also genetically interact with different types of repeat nucleoporins, such as Nup116p, Nup159p, Nsp1p, and Rip1p/Nup40p. These data suggest a model in which nuclear mRNA export requires the Mex67p/Mtr2p heterodimeric complex to directly contact several repeat nucleoporins, organized in different nuclear pore complex subcomplexes, as it carries the mRNP cargo through the nuclear pore.

Key Words: nucleocytoplasmic transport, Nup116, Nup159, Rip1, nuclear pore complex


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