Vertebrate TAP is a nuclear mRNA export factor homologous to yeast Mex67p. The middle domain of TAP binds directly to p15, a protein related to the nuclear transport factor 2 (NTF2), whereas its C-terminal domain interacts with various nucleoporins, the components of the nuclear pore complex (NPC). Here, we report that the middle domain of TAP is also similar to NTF2, as well as to regions in Ras-GAP SH3 domain binding protein (G3BP) and some plant protein kinases. Based on the known three-dimensional structure of NTF2 homodimer, a heterodimerization model of TAP and p15 could be inferred. This model was confirmed by site-directed mutagenesis of residues located at the dimer interface. Furthermore, the C-terminus of TAP was found to contain a ubiquitin-associated (UBA) domain. By site-directed mutagenesis we show that a conserved loop in this domain plays an essential role in mediating TAP-nucleoporin interaction.
Pubmed ID: 11256625 RIS Download
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A freeware Macintosh program for simulating and testing polymerase chain reactions (PCRs) that can also be used as a tool for designing primers by evaluating candidates. It's a program to simulate the polymerase chain reaction. You specify a target sequence and primers, and it predicts the result. It's useful for planning experiments, testing primers and teaching about PCR. Amplify draws a diagram of the predicted results showing all expected primer matches and amplified fragments. Clicking on any of these objects gives additional information about them.
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