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Vol. 15, No. 10, pp. 1194-1205, May 15, 2001
1 Howard Hughes Medical Institute and 2 Department
of Genetics, Duke University Medical Center, Durham, North Carolina
27710, USA; 3 Waksman Institute and Department of Chemistry,
Rutgers University, Piscataway, New Jersey 08854, USA
The Tap protein mediates the sequence-specific nuclear export of
mRNAs bearing the retroviral constitutive transport element (CTE) and
also plays a critical role in the sequence nonspecific export of
cellular mRNAs. Previously, we have demonstrated that CTE function
displays species specificity, that is, the CTE functions in human but
not quail cells. Here, we demonstrate that quail Tap fails to support
CTE function because it cannot bind the CTE. However, changing a single
residue in quail Tap, glutamine 246, to arginine, the residue found in
human Tap, rescues both CTE function and CTE binding. This residue,
which is located on the exterior of a recently reported molecular
structure of Tap, defines a surface on Tap that is critical for CTE
binding. These data emphasize the potential importance of cross-species
genetic complementation in the identification and characterization of
cellular factors that are critical for different aspects of viral replication.
[Key Words: Gene regulation; nuclear export; retrovirus; RNA binding]
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