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Vol. 14, Issue 3, 836-847, March 2003
and
*Department of Biological Chemistry and Molecular
Pharmacology, Harvard Medical School and Dana Farber Cancer Institute,
Boston, Massachusetts 02115; and In eukaryotes, mRNAs are transcribed in the nucleus and exported to
the cytoplasm for translation to occur. Messenger RNAs complexed with
proteins referred to as ribonucleoparticles are recognized for
nuclear export in part by association with Mex67, a key
Saccharomyces cerevisiae mRNA export factor and homolog of human TAP/NXF1. Mex67, along with its cofactor Mtr2, is thought to
promote ribonucleoparticle translocation by interacting directly with
components of the nuclear pore complex (NPC). Herein, we show that the
nuclear pore-associated protein Sac3 functions in mRNA export. Using a
mutant allele of MTR2 as a starting point, we have
identified a mutation in SAC3 in a screen for synthetic lethal interactors. Loss of function of SAC3 causes a
strong nuclear accumulation of mRNA and synthetic lethality with a
number of mRNA export mutants. Furthermore, Sac3 can be
coimmunoprecipitated with Mex67, Mtr2, and other factors involved in
mRNA export. Immunoelectron microscopy analysis shows that Sac3
localizes exclusively to cytoplasmic fibrils of the NPC. Finally, Mex67
accumulates at the nuclear rim when SAC3 is mutated,
suggesting that Sac3 functions in Mex67 translocation through the NPC.
M.E.
Müller Institute for Structural Biology, Biozentrum, University
of Basel, 4056 Basel, Switzerland
Philipps-University Marburg,
Institute for Molecular Biology and Tumor Research,
Emil-Mannkopff-Stra
e 2, 35033 Marburg, Germany;
§Department of Genetics, Harvard Medical School and
Massachusetts General Hospital, Boston, MA 02114.
Corresponding author. E-mail address:
pamela_silver{at}dfci.harvard.edu.
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