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

M T Teixeira; S Siniossoglou; S Podtelejnikov; J C Bénichou; M Mann; B Dujon; E Hurt; E Fabre

doi:10.1093/emboj/16.16.5086

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

EMBO J. 1997 Aug 15;16(16):5086-97. doi: 10.1093/emboj/16.16.5086.

Authors

M T Teixeira¹, S Siniossoglou, S Podtelejnikov, J C Bénichou, M Mann, B Dujon, E Hurt, E Fabre

Affiliation

¹ Unité de Génétique Moléculaire des levures (URA 1300 CNRS and UPR 927 Univ. P M Curie), Institut Pasteur, Département des Biotechnologies, Paris, France.

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Biological Transport / physiology
Blotting, Western
Electrophoresis, Polyacrylamide Gel
Fungal Proteins / analysis
Fungal Proteins / chemistry*
Fungal Proteins / genetics
Fungal Proteins / metabolism*
Microscopy, Electron
Molecular Sequence Data
Mutagenesis, Site-Directed / genetics
Nuclear Envelope / chemistry*
Nuclear Envelope / metabolism
Nuclear Pore Complex Proteins*
Nuclear Proteins / metabolism
Protein Processing, Post-Translational
RNA, Fungal / metabolism
RNA, Messenger / metabolism
RNA-Binding Proteins / analysis
RNA-Binding Proteins / chemistry*
RNA-Binding Proteins / genetics
RNA-Binding Proteins / metabolism*
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / metabolism
Saccharomyces cerevisiae Proteins*
Sequence Homology, Amino Acid
Staphylococcal Protein A / genetics
Yeasts / genetics
Yeasts / growth & development
Yeasts / metabolism

Substances

Fungal Proteins
NUP145 protein, S cerevisiae
NUP84 protein, S cerevisiae
Nuclear Pore Complex Proteins
Nuclear Proteins
RNA, Fungal
RNA, Messenger
RNA-Binding Proteins
Recombinant Fusion Proteins
Saccharomyces cerevisiae Proteins
Staphylococcal Protein A