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MBC in Press, published online ahead of print September 14, 2005
Mol. Biol. Cell 10.1091/mbc.E05-06-0527

A more recent version of this article appeared on November 1, 2005
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Submitted on June 13, 2005
Revised on August 16, 2005
Accepted on September 1, 2005

Pml39, a Novel Protein of the Nuclear Periphery Required for Nuclear Retention of Improper mRNPs

Benoit Palancade,* Michela Zuccolo,* Sophie Loeillet,{dagger} Alain Nicolas,{dagger} and Valérie Doye*

*Pores Nucléaires et Transport Nucléocytoplasmique, UMR144 CNRS and {dagger}Recombinaison et Instabilité Génétique, UMR7147 CNRS/Université Pierre et Marie Curie, Institut Curie, Section de Recherche, 75248 Paris Cedex 05, France

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 nup60{Delta} mutant, Pml39 is mislocalized together with Mlp1 and Mlp2 in intranuclear foci that also recruit Nab2. Moreover, pml39{Delta} 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.

Address correspondence to: Benoit Palancade (palancad{at}curie.fr)




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