Identification of a new transmembrane nuclear pore protein in Aspergillus nidulans using global proteomic analysis

Ref ID: 18369

Author:

Aysha H. Osmani, Hui-Lin
Liu, Colin P. De Souza and Stephen A. Osmani.

Author address:

The Ohio State University, Columbus, OH, USA. (osmani.2@osu.edu)

Full conference title:

Asperfest 8

Abstract:

We have previously reported the unexpected finding that in Aspergillus nidulans removal of all three fungal transmembrane nuclear pore complex (NPC)
proteins (An-Ndc1, An-Pom152, and An-Pom34) does not cause lethality (Liu et al., 2009 MBC 20, 616-630). This suggests either that transmembrane
proteins are not required for NPC function or that additional transmembrane NPC proteins remain to be discovered. To address this issue we have
completed a global proteomic analysis of A. nidulans Nups (NPC proteins) using affinity purification and mass spectrometry analysis. This approach
involved endogenously tagging >40 different proteins and completing LC/MS/MS analysis of >100 purified samples. The data set has allowed
identification of numerous proteins that interact with NPCs including an orthologue of a new transmembrane Nup (Pom33) recently discovered in budding
yeast (Chadrin et al., 2010 JCB 189, 795-811). An- Pom33 purified with An-Ndc1. Using GFP tagging and deletion analysis we have asked if An-Pom33
is a newtransmembrane Nup in A. nidulans. As expected of a transmembrane Nup, An-Pom33-GFP locates to the nuclear envelope throughout interphase,
concentrating at spindle pole bodies during mitosis in a manner similar to An-Ndc1. In addition, An-Pom33 is also present in the cytoplasm in an ER-like
structure. Removal of An-Pom33 does not cause lethality but the quadruple transmembrane Nup mutant (lacking An-Ndc1, An-Pom152, An-Pom34, and
An-Pom33) is inviable. Pairwise deletions revealed that lack of An-Pom33 with lack of An-Ndc1 is the only lethal combination. This study identifies
An-Pom33 as a conserved transmembrane Nup that functions redundantly with An-Ndc1. (Supported by NIH grant GM042564)

Abstract Number: 47)

Conference Year: 2011

Link to conference website: NULL

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