Ruprecht-Karls-Universität Heidelberg
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Oezbek0218 - Scientist (f/m) / PhD position
Project no:
Oezbek0218

Project leader:

Project supervisor:
Özbek, Suat
Application deadline:
28. Feb 2018
Start of PhD project:
1. Apr 2018

Project description:

Title:
Novel molecular factors in nematocyst assembly and morphogenesis II
Summary:
The cnidarian nematocyst, used for predation and defense, is the most complex organelle in the animal kingdom. Its ultra-fast, harpoon-like discharge, which is accompanied by a release of toxins, requires molecular factors with unusual biomechanical properties. Our previous analysis of the Hydra nematocyst proteome revealed more than 400 molecular factors constituting the nematocyst. Among these, we have characterized in detail the family of minicollagens and the elastic protein Cnidoin, which in concert are responsible for the high structural resilience and kinetic energy release during the discharge process. The present project is focused on novel molecular factors involved in the assembly of the nematocyst tubule structure, which is the most elaborate and innovative part of the organelle. The project blends proteomic screens with high-resolution imaging of expression patterns und hardcore biochemical studies.
References:
Ballistic “nematocysts” in dinoflagellates represent a new extreme in organelle complexity. Sci. Adv. 2017;3: e1602552.
Minicollagen cysteine-rich domains encode distinct modes of polymerization to form stable nematocyst capsules. Sci Rep. 6:25709.
A fast recoiling silk-like elastomer facilitates nanosecond nematocyst discharge. BMC biology. 13:3.
Proteome of Hydra nematocyst. J Biol Chem. Mar 23;287(13):9672-81.
Morphological and molecular analysis of the Nematostella vectensis cnidom. PLoS One.;6(7):e22725.
Nematogalectin, a nematocyst protein with GlyXY and galectin domains, demonstrates nematocyte-specific alternative splicing in Hydra. Proc Natl Acad Sci U S A. Oct 26;107(43):18539-44.
A non-sulfated chondroitin stabilizes membrane tubulation in cnidarian organelles. J Biol Chem. Aug 13;285(33):25613-23.
Continuous molecular evolution of protein domain structures by single amino acid changes. Current Biology, January 23;17:173-178.
Methods that will be used:
molecular biology, protein biochemistry, proteomics, bioinformatics, immunocytochemistry, fluorescence microscopy, in situ hybridization.
Cooperation partners:
Personal qualifications:
Experience in bioinformatics, molecular biology, protein biochemistry, and advanced light microscopy. Experience with cnidarian model systems is advantageous, but not compulsory. We are looking for a highly motivated and skilled candidate with genuine interest in evolutionary biology.
Keywords: