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Sci Rep. 2018 Feb 26;8(1):3611. doi: 10.1038/s41598-018-21628-y.

Cytoplasmic Transport Machinery of the SPF27 Homologue Num1 in Ustilago maydis.

Author information

1
Institute of Applied Physics, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
2
Institute of Nanotechnology, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
3
Department of Genetics, Institute of Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
4
Institute of Microbiology, Cluster of Excellence on Plant Sciences, Heinrich-Heine-University, Düsseldorf, Germany.
5
Institute of Applied Physics, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany. uli@uiuc.edu.
6
Institute of Nanotechnology, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany. uli@uiuc.edu.
7
Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA. uli@uiuc.edu.
8
Institute of Toxicology and Genetics, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany. uli@uiuc.edu.
9
Department of Genetics, Institute of Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany. joerg.kaemper@kit.edu.

Abstract

In the phytopathogenic basidiomycete Ustilago maydis, the Num1 protein has a pivotal function in hyphal morphogenesis. Num1 functions as a core component of the spliceosome-associated Prp19/CDC5 complex (NTC). The interaction of Num1 with the kinesin motor Kin1 suggests a connection between a component of the splicing machinery and cytoplasmic trafficking processes. Previously it was shown that Num1 localizes predominantly in the nucleus; however, due to the diffraction-limited spatial resolution of conventional optical microscopy, it was not possible to attribute the localization to specific structures within the cytoplasm. We have now employed super-resolution localization microscopy to visualize Num1 in the cytoplasm by fusing it to a tandem dimeric Eos fluorescent protein (tdEosFP). The Num1 protein is localized within the cytoplasm with an enhanced density in the vicinity of microtubules. Num1 movement is found predominantly close to the nucleus. Movement is dependent on its interaction partner Kin1, but independent of Kin3. Our results provide strong evidence that, in addition to its involvement in splicing in the nucleus, Num1 has an additional functional role in the cytosol connected to the Kin1 motor protein.

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