Proteomics

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Analysis of the Putative Nucleoporin POM33 in the Filamentous Fungus Sordaria macrospora

ABSTRACT: The POM33 protein of Sordaria macrospora is a nucleoporin considered of being an ER-protein that may function in ER-shaping and organization. In this study, we performed TagRFP-T pulldown experiments in S. macrospora strains expressing either POM33-TagRFP-T or the free TagRFP-T as control to identify putative POM33 interaction partners. Since with the SmSTRIPAK-component SCI1, POM33 was found, we expected with this approach to vice versa pull down SCI1. The results of the LC/MS analysis revealed mainly proteins that are located at the ER-membrane where they have functions in fatty acid biosynthesis, sterol biosynthesis, lipid metabolism or ER-shaping and maintaining its organization. These results gave us an overall picture about putative interactions of POM33 to specify its localization and function in S. macrospora hyphae.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Sordaria Macrospora

SUBMITTER: Oliver Valerius  

LAB HEAD: Stefanie Pöggeler

PROVIDER: PXD026253 | Pride | 2021-08-23

REPOSITORIES: Pride

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Analysis of the Putative Nucleoporin POM33 in the Filamentous Fungus <i>Sordaria macrospora</i>.

Groth Anika A   Schmitt Kerstin K   Valerius Oliver O   Herzog Britta B   Pöggeler Stefanie S  

Journal of fungi (Basel, Switzerland) 20210824 9

In the filamentous fungus <i>Sordaria macrospora</i> (Sm), the STRIPAK complex is required for vegetative growth, fruiting-body development and hyphal fusion. The SmSTRIPAK core consists of the striatin homolog PRO11, the scaffolding subunit of phosphatase PP2A, SmPP2AA, and its catalytic subunit SmPP2Ac1. Among other STRIPAK proteins, the recently identified coiled-coil protein SCI1 was demonstrated to co-localize around the nucleus. Pulldown experiments with SCI identified the transmembrane nu  ...[more]

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