International Leibniz Research School for Microbial and Biomolecular Interactions - ILRS Jena
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International Leibniz Research School

for Microbial and Biomolecular Interactions ILRS Jena

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Dominik Senftleben
Amin, Shayista
Behnken, Swantje
Brandes, Susanne
Chen, Qian
Eberhardt, Hannes
Enghardt, Tina
Fischer, Juliane
Funk, Alexander
Graupner, Katharina
Heddergott, Christoph
Horn, Fabian
Jbeily, Nayla
Jetha, Khushboo
Kopka, Isabell
Kroll, Kristin
Machanda, Himanshu
MacNelly, Anita
Mauß, Michaela
Mayer, François
Mingo, Felix
Mohan, Karthik Mohan
Mohebbi, Sara
Müller, Christiane
Müller, Sebastian
Ramachandra, Shruthi
Sarkar, Sarbani
Schwenk, Daniel
Seddigh, Pegah
Senftleben, Dominik
Stippa, Selina
Thywißen, Andreas
Weinhold, Arne
 

Dominik Senftleben

Personal Data:
Country of Origin: Germany
Start of PhD: November 2009
Institution: FSU

PhD Project:
A surface hydrophobin in ectomycorrhiza interaction

Supervisor(s): E. Kothe (FSU), A.A. Brakhage (HKI)

Abstract
Hydrophobins are small secreted proteins with low sequence homology. However, all proteins contain eight cysteines, which form disulfide bridges. They are divided into two classes, depending on their solubility and have a broad range of functions like in processes of growth and development of filamentous fungi, e.g. formation of aerial structures. Mutual symbiosis like ectomycorrhiza is based on differential gene expression. This was shown for hydrophobin tthyd1 which is upregulated in the Hartig’net in the interaction of Tricholoma terreum with pine. We investigate hydrophobins in Tricholoma vaccinum, a widely spread basidiomycete (agaricales – tricholomataceae) – forming ectomycorrhiza with spruce. The aim is to analyze in which stage of the life cycle respectively symbiotic interaction hydrophobins are produced, what kind of role they play (heterologous expression) with respect to function in the symbiotic tissue (RNAi) and if they are regulated in relation to heavy metal response. Apart from the hypothesis of the heavy metal response, the regulation of hydrophobins will be analyzed through repression of an RGS and Gα protein.

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