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Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins.

The EMBO journal | Aug 15, 1997

http://www.ncbi.nlm.nih.gov/pubmed/9305650

Nup145p is an essential yeast nucleoporin involved in nuclear export of polyadenylated RNAs. We demonstrate here that Nup145p is cleaved in vivo to yield two functionally distinct domains: a carboxy-terminal domain (C-Nup145p) which is located at the nuclear pore complex (NPC) and assembles into the Nup84p complex, and a GLFG-containing amino-terminal domain (N-Nup145p) which is not part of this complex. Whereas the essential C-Nup145p accomplishes the functions required for efficient mRNA export and normal NPC distribution, N-Nup145p, which is homologous to the GLFG-containing nucleoporins Nup100p and Nup116p, is not necessary for cell growth. However, the N-Nup145p becomes essential in a nup188 mutant background. Strikingly, generation of a free N-domain is a prerequisite for complementation of this peculiar synthetic lethal mutant. These data suggest that N- and C-domains of Nup145p perform independent functions, and that the in vivo cleavage observed is of functional importance.

Pubmed ID: 9305650 RIS Download

Mesh terms: Amino Acid Sequence | Biological Transport | Blotting, Western | Electrophoresis, Polyacrylamide Gel | Fungal Proteins | Microscopy, Electron | Molecular Sequence Data | Mutagenesis, Site-Directed | Nuclear Envelope | Nuclear Pore Complex Proteins | Nuclear Proteins | Protein Processing, Post-Translational | RNA, Fungal | RNA, Messenger | RNA-Binding Proteins | Recombinant Fusion Proteins | Saccharomyces cerevisiae Proteins | Sequence Homology, Amino Acid | Staphylococcal Protein A | Yeasts

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