IndraLab

Statements


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"Its nuclear export is prevented through the presence of Hrp1, which in the absence of Rna14 cannot bind Mex67 and then functions as a retention factor, as the absence of Mex67 from Hrp1 is detected by Mlp1 at the NPC, and transfer to the cytoplasm is prevented."

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"To ensure that Hrp1 is able to directly bind Mex67 and does not simply interact with the export receptor due to being present in the same complex, we precipitated Hrp1 expressed from yeast cells in vivo and analyzed the binding of purified Mex67–Mtr2 expressed from Escherichia coli in vitro (Figure 1H, I)."

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"Thus, it seems that defects in the cleavage reaction prevent binding between Hrp1 and Mex67, which would inhibit the nuclear export of the bound mRNA."

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"These findings support the idea that controlled Mex67 recruitment by Hrp1 determines nuclear export and that only Rna14-bound Hrp1 can interact with the export receptor.If this model would be true, one would expect that Hrp1 is still bound to cleavage-defective mRNAs."

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"Reassuringly, binding between Hrp1 and Mex67 was detected."