Palancade B, et al. (2005) Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles. Mol Biol Cell 16(11):5258-68
Abstract: Monitoring Editor: Susan Wente Using a genetic screen, we have identified a previously uncharacterized S. cerevisiae ORF (renamed Pml39) that displays a specific interaction with nucleoporins of the Nup84 complex. Localization of a Pml39-GFP fusion and two-hybrid studies revealed that Pml39 is mainly docked to a subset of nuclear pore complexes opposite to the nucleolus through interactions with Mlp1 and Mlp2. The absence of Pml39 leads to a specific leakage of unspliced mRNAs that is not enhanced upon MLP1 deletion. In addition, overexpression of PML39-GFP induces a specific trapping of mRNAs transcribed from an intron-containing reporter and of the hnRNP Nab2 within discrete nuclear domains. In a nup60Delta mutant, Pml39 is mislocalized together with Mlp1 and Mlp2 in intranuclear foci that also recruit Nab2. Moreover, pml39Delta partially rescues the thermosensitive phenotypes of mRNP assembly mutants, indicating that pml39 deletion also bypasses the requirement for normally assembled mRNPs. Altogether, these data indicate that Pml39 is an upstream effector of the Mlps, involved in the retention of improper mRNPs in the nucleus before their export.
|Status: Published||Type: Journal Article||PubMed ID: 16162818|
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|Non-Fungal Related Genes/Proteins|
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