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22Nd Fungal Genetics Conference at Asilomar Fungal Genetics Reports Volume 50 Article 18 22nd Fungal Genetics Conference at Asilomar Fungal Genetics Conference Follow this and additional works at: https://newprairiepress.org/fgr This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License. Recommended Citation Fungal Genetics Conference. (2003) "22nd Fungal Genetics Conference at Asilomar," Fungal Genetics Reports: Vol. 50, Article 18. https://doi.org/10.4148/1941-4765.1164 This Supplementary Material is brought to you for free and open access by New Prairie Press. It has been accepted for inclusion in Fungal Genetics Reports by an authorized administrator of New Prairie Press. For more information, please contact [email protected]. 22nd Fungal Genetics Conference at Asilomar Abstract Abstracts from the 2003 Fungal Genetics Conference at Asilomar This supplementary material is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol50/iss1/18 : 22nd Fungal Genetics Conference at Asilomar 22nd Fungal Genetics Conference at Asilomar Plenary Session Abstracts Microtubules in polar growth of Ustilago maydis Gero Steinberg Polar growth of yeasts and filamentous fungi depends on cytoskeleton-based transport of vesicles and protein complexes towards the expanding cell pole. While solid evidence exists for a central function of F-actin in fungal growth, the importance of the tubulin cytoskeleton is by far less understood. In vivo observation of microtubules in growing cells of Ustilago maydis revealed that the dynamic ends ("plus"-ends) of these tubulin polymers are growing towards the cell poles, while cytoplasmic microtubule organizing centers focus the microtubule minus-ends at the neck region. This microtubule orientation suggests that minus-end directed dynein motors support transport towards the neck, whereas plus-end directed kinesin motors might be required for transport towards the poles of the cell. This concept is supported by the recent identification of the transport machinery for microtubule-based traffic of early endosomes that depends on both a Kif1A-like kinesin and cytoplasmic dynein. Interestingly, a balance of the activity of these motors determines the cell cycle-dependent formation of endosome clusters at both cell poles, where the endosomes apparently support polar growth, bipolar budding and septation. However, it emerges that, in addition to their function in membrane transport, both motors influence the organization of their transport "tracks" by modifying dynamic parameters of microtubules in U. maydis. Understanding this dual function of motors will be a fascinating future challenge, and might be key to the understanding of the role of microtubules in polar fungal growth. Genetics analysis of the regulation of cytoplasmic dynein in Neurospora. M. Plamann, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110-2499. Cytoplasmic dynein is the most complex of the cytoplasmic microtubule-associated motor proteins, and it has been shown to be required for retrograde vesicle transport and the movement and positioning of nuclei in fungi. Analysis of cytoplasmic dynein from mammals reveals that at least 16 different gene products are required for formation of the dynein motor, the dynein activator complex dynactin, and the LIS1 complex, required for dynein function. Examination of the recently completed genome sequence of Neurospora crassa reveals a high degree of conservation for nearly all these gene products. We have developed a simple genetic system for the isolation of mutants defective in cytoplasmic dynein function. We have shown previously that most of the genes defined through this screen encode subunits of cytoplasmic dynein or dynactin. We have now cloned all but one of the genes defined by our screen. Interestingly, we have not identified mutations in four genes encoding known dynein/dynactin subunits, although genomic sequence data suggests that apparent orthologs are present in N. crassa. In addition, we have also defined two genes that have not previously been implicated as required for dynein/dynactin function. Septins in Aspergillus nidulans. Michelle Momany. Department of Plant Biology, University of Georgia, Athens, GA. USA Septins form scaffolds that organize division sites and areas of new growth in fungi and animals. Many proteins critical for cytokinesis and cell cycle regulation depend upon septins for proper localization. Five septins (AspA-AspE) have been identified in A. nidulans. AspB localizes to forming septa and conidiophore layers. It also localizes to emerging branches where it may play a role in cell cycle regulation of subapical compartments. Deletion of AspB is lethal and deletion of other septins results in branched conidiophores. Nuclear migration in Aspergillus nidulans: Motors, microtubules and more Reinhard Fischer, Max-Planck-Institute for terrestrial Microbiology and Philipps-University Marburg, Karl-von- Frisch-Str., D-35043 Marburg, Germany. Published by New Prairie Press, 2017 1 Fungal Genetics Reports, Vol. 50 [2003], Art. 18 Nuclei migrate through growing hyphae of A. nidulans with a similar speed as hyphae elongate. However, nuclear behavior is much more complex than just a simple tipward travel. They oscillate on their way around a certain position, move backwards for short time periods, enter newly formed branches, devide while moving and populate the reproductive structures such as asexual and sexual spores. The movement requires the microtubule-dependent motor dynein and an intact microtubule cytoskeleton. We asked whether kinesins may play a role in the migration process and isolated three novel genes. The corresponding proteins displayed similarity to conventional kinesin and S. cerevisiae Kip2 (KipA) and Kip3 (KipB). Deletion analyses revealed that only conventional kinesin had an effect on nuclear migration. KipA-mutation affected polarized growth, likely through the positioning of the Spitzenkörper and KipB appeared to be involved in mitosis and meiosis. Likewise, the latter protein localised to cytoplasmic and to mitotic microtubules. In addition to motor proteins and the microtubule tracks, nuclear positioning in A. nidulans requires two proteins, ApsA and ApsB. In vivo localisation studies revealed that ApsA forms a protein gradient along the cortex. This gradient depends on the actin cytoskeleton to be maintained. In contrast, ApsB localised to the nucleus and appeared to be associated to the spindle pole body. Simultaneous observation of nuclear movement, microtubule dynamics and ApsB behavior suggested that ApsB might be invovled in the movement of nuclei along microtubule filaments. We observed migration of the nucleus along one microtubule filament towards the plus and the minus end of one microtubule, suggesting the involvement of motors with different polarity. We believe that this movement represents one possibility how nuclei can be translocated within a hyphal cell. Fungal mitosis, closed or open? Colin De Souza and Stephen Osmani. Department of Molecular Genetics, the Ohio State University, Columbus, OH43210, USA The nuclear envelope is broken down at mitosis in higher eukaryotes leading to an "open" mitosis but in fungi the mitotic apparatus is enclosed within a nuclear envelope and so remains "closed". Recent work on the NIMA kinase of Aspergillus nidulans suggests that the closed mitosis of fungi may be more open than previously recognized. We have determined the location of NIMA in real time through the cell cycle. At G2 it is excluded from the nucleus and at early mitosis it locates transiently to the nuclear pore complex (NPC) before locating to the nucleus. The C- terminal regulatory domain of NIMA is sufficient to target GFP to the NPC and this domain acts in a dominant negative fashion, delaying entry into mitosis. The data support a mitotic role for NIMA at the NPC. We have previously isolated sonA as a NPC protein that could specifically suppress nimA1. A second extragenic suppressor of nimA1 has now been cloned (sonB) and identified as a NPC protein with homology to human Nup98/Nup96 proteins. Not only do mutations of sonA and sonB suppress the nimA1 mutation, these two NPC proteins physically interact as revealed by co-immunoprecipitation experiments. Moreover, the interaction between SONA and SONB is reduced by the sonB1 mutation which is within a domain of SONB responsible for binding to SONA. Thus, both genetic and biochemical data indicate that NIMA and two interacting NPC proteins play a role in mitotic regulation. The dynamic localization of SONA and SONB further implicates these proteins in mitotic regulation, as both are precipitously lost from the NPC at mitotic onset and then locate back to the NPC at mitotic exit. These studies reveal for the first time that the protein makeup of the NPC radically changes during a closed fungal mitosis. We propose that these changes open the NPC to allow protein diffusion either in or out of nuclei during mitosis. Proteins which have an affinity for nuclear components concentrate within nuclei, for example tubulin and NIMA. Other nuclear proteins, with no affinity for nuclear components, escape from nuclei during mitosis into the cytoplasm. As daughter nuclei are produced, and SONA and SONB relocate to the NPC, normal nuclear transport is reestablished. This then plays a role in relocating proteins by active transport. Therefore, perhaps the "closed" mitosis of fungi is more open then previously realized. Distinct endophyte genome evolution associated
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