The Aspergillus nidulans Kinesin8208;3 Tail Is Necessary And Sufficient To Recognize Modified Microtubules

Ref ID: 18441


Constanze Seidel, Nadine Zekert, Reinhard Fischer

Author address:

Karlsruhe Institute of Technology, Institute for Applied Biosciences, Dept. of Microbiology

Full conference title:

11 th European Conference on Fungal Genetics


Posttranslational microtubule modifications are numerous; however, the biochemical and cell biological roles of
those modifications remain mostly an enigma. The Aspergillus nidulans kinesin8208;3 UncA uses preferably modified
MTs as tracks for vesicle transportation. Here, we show that a positively charged region in the tail of UncA (amino
acids 1316 to 1402) is necessary for the recognition of modified MTs. Chimeric proteins composed of the kinesin8208;1
motor domain and the UncA tail displayed the same specificity as UncA, suggesting that the UncA tail is sufficient
to establish specificity. Interaction between the UncA tail and alpha8208;tubulin was shown using a yeast two8208;hybrid
assay and in A. nidulans by bimolecular fluorescence complementation (BiFC). Our data show that specificity
determination depends on the tail rather than the motor domain, as has been demonstrated for kinesin 1 in
neuronal cells.
In a non8208;targeted Y2H approach interaction partners of this region were identified, because they are most likely
involved in the recognition of MT subpopulations. Several candidates were confirmed using BiFC. Two are
associated with vesicles; one is a predicted siderophore uptake transmembrane transporter and the other one was
previously shown to be involved in ER to Golgi vesicle8208;mediated transport. The deletion of another fished
interactor with similarity to Phosphatidylinositol 38208; & 48208;kinase family showed strongly reduced growth. Further
characterization of a potentinal role in regulating the activity and specificity of UncA is in progress.

Abstract Number: PS1.4

Conference Year: 2012

Link to conference website:

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